© 2022 - Robin Ohm - Utrecht University - The Netherlands
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| Protein ID | AgabiH97|056320 |
| Gene name | |
| Location | scaffold_3:889628..892369 |
| Strand | + |
| Gene length (bp) | 2741 |
| Transcript length (bp) | 1824 |
| Coding sequence length (bp) | 1824 |
| Protein length (aa) | 608 |
| PFAM Domain ID | Short name | Long name | E-value | Start | End |
|---|---|---|---|---|---|
| PF00441 | Acyl-CoA_dh_1 | Acyl-CoA dehydrogenase, C-terminal domain | 2.2E-41 | 451 | 598 |
| PF06090 | Ins_P5_2-kin | Inositol-pentakisphosphate 2-kinase | 2.5E-37 | 1 | 197 |
| PF02771 | Acyl-CoA_dh_N | Acyl-CoA dehydrogenase, N-terminal domain | 5.3E-32 | 228 | 339 |
| PF02770 | Acyl-CoA_dh_M | Acyl-CoA dehydrogenase, middle domain | 1.7E-22 | 344 | 439 |
| PF08028 | Acyl-CoA_dh_2 | Acyl-CoA dehydrogenase, C-terminal domain | 1.2E-13 | 473 | 579 |
| Swissprot ID | Swissprot Description | Start | End | E-value |
|---|---|---|---|---|
| sp|Q75IM9|IVD_ORYSJ | Isovaleryl-CoA dehydrogenase, mitochondrial OS=Oryza sativa subsp. japonica GN=Os05g0125500 PE=2 SV=2 | 205 | 599 | 3.0E-176 |
| sp|Q9JHI5|IVD_MOUSE | Isovaleryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Ivd PE=1 SV=1 | 211 | 600 | 4.0E-171 |
| sp|Q5RBD5|IVD_PONAB | Isovaleryl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=IVD PE=2 SV=1 | 207 | 600 | 7.0E-171 |
| sp|P26440|IVD_HUMAN | Isovaleryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=IVD PE=1 SV=1 | 212 | 600 | 5.0E-170 |
| sp|Q9FS88|MBCD_SOLTU | 2-methylacyl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum GN=2MBCD PE=1 SV=2 | 227 | 602 | 2.0E-169 |
| Swissprot ID | Swissprot Description | Start | End | E-value |
|---|---|---|---|---|
| sp|Q75IM9|IVD_ORYSJ | Isovaleryl-CoA dehydrogenase, mitochondrial OS=Oryza sativa subsp. japonica GN=Os05g0125500 PE=2 SV=2 | 205 | 599 | 3.0E-176 |
| sp|Q9JHI5|IVD_MOUSE | Isovaleryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Ivd PE=1 SV=1 | 211 | 600 | 4.0E-171 |
| sp|Q5RBD5|IVD_PONAB | Isovaleryl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=IVD PE=2 SV=1 | 207 | 600 | 7.0E-171 |
| sp|P26440|IVD_HUMAN | Isovaleryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=IVD PE=1 SV=1 | 212 | 600 | 5.0E-170 |
| sp|Q9FS88|MBCD_SOLTU | 2-methylacyl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum GN=2MBCD PE=1 SV=2 | 227 | 602 | 2.0E-169 |
| sp|P12007|IVD_RAT | Isovaleryl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Ivd PE=1 SV=2 | 207 | 600 | 1.0E-168 |
| sp|Q9FS87|IVD_SOLTU | Isovaleryl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum GN=IVD PE=1 SV=2 | 229 | 599 | 2.0E-168 |
| sp|Q3SZI8|IVD_BOVIN | Isovaleryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=IVD PE=2 SV=1 | 203 | 600 | 2.0E-166 |
| sp|Q9SWG0|IVD_ARATH | Isovaleryl-CoA dehydrogenase, mitochondrial OS=Arabidopsis thaliana GN=IVD PE=1 SV=2 | 229 | 599 | 4.0E-166 |
| sp|P45857|ACDB_BACSU | Acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) GN=mmgC PE=2 SV=3 | 227 | 597 | 2.0E-85 |
| sp|P45867|ACDA_BACSU | Acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) GN=acdA PE=2 SV=1 | 227 | 597 | 9.0E-85 |
| sp|P52042|ACDS_CLOAB | Acyl-CoA dehydrogenase, short-chain specific OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) GN=bcd PE=1 SV=1 | 227 | 595 | 5.0E-82 |
| sp|O34421|ACDC_BACSU | Probable acyl-CoA dehydrogenase YngJ OS=Bacillus subtilis (strain 168) GN=yngJ PE=3 SV=1 | 227 | 599 | 4.0E-77 |
| sp|Q07417|ACADS_MOUSE | Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acads PE=1 SV=2 | 234 | 596 | 2.0E-75 |
| sp|Q06319|ACDS_MEGEL | Acyl-CoA dehydrogenase, short-chain specific OS=Megasphaera elsdenii PE=1 SV=1 | 227 | 596 | 1.0E-74 |
| sp|P15651|ACADS_RAT | Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acads PE=1 SV=2 | 234 | 596 | 2.0E-74 |
| sp|Q5RAS0|ACADS_PONAB | Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=ACADS PE=2 SV=1 | 240 | 595 | 4.0E-74 |
| sp|P16219|ACADS_HUMAN | Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADS PE=1 SV=1 | 240 | 595 | 2.0E-73 |
| sp|Q9DBL1|ACDSB_MOUSE | Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadsb PE=1 SV=1 | 217 | 600 | 6.0E-73 |
| sp|P70584|ACDSB_RAT | Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadsb PE=1 SV=1 | 227 | 600 | 1.0E-72 |
| sp|P45954|ACDSB_HUMAN | Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADSB PE=1 SV=1 | 227 | 600 | 4.0E-72 |
| sp|Q5RF40|ACDSB_PONAB | Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=ACADSB PE=2 SV=1 | 227 | 600 | 6.0E-72 |
| sp|P79273|ACADS_PIG | Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Sus scrofa GN=ACADS PE=2 SV=1 | 234 | 596 | 6.0E-71 |
| sp|G3KIM8|ACRC_CLOPR | Acryloyl-CoA reductase (NADH) OS=Clostridium propionicum GN=acrC PE=1 SV=1 | 227 | 598 | 4.0E-70 |
| sp|Q5EAD4|ACDSB_BOVIN | Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADSB PE=2 SV=1 | 227 | 597 | 1.0E-69 |
| sp|Q3ZBF6|ACADS_BOVIN | Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADS PE=1 SV=1 | 234 | 596 | 1.0E-69 |
| sp|Q54RR5|ACDSB_DICDI | Probable short/branched chain specific acyl-CoA dehydrogenase OS=Dictyostelium discoideum GN=acadsb PE=3 SV=1 | 224 | 598 | 5.0E-68 |
| sp|Q54IM8|ACAD8_DICDI | Isobutyryl-CoA dehydrogenase, mitochondrial OS=Dictyostelium discoideum GN=acad8 PE=3 SV=1 | 212 | 604 | 1.0E-65 |
| sp|P9WQG1|ACDP_MYCTU | Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=fadE25 PE=1 SV=1 | 227 | 597 | 2.0E-65 |
| sp|P9WQG0|ACDP_MYCTO | Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=fadE25 PE=3 SV=1 | 227 | 597 | 2.0E-65 |
| sp|P63428|ACDP_MYCBO | Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=fadE25 PE=3 SV=1 | 227 | 597 | 2.0E-65 |
| sp|Q2LQN9|CH1CO_SYNAS | Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase OS=Syntrophus aciditrophicus (strain SB) GN=SYN_02587 PE=1 SV=1 | 227 | 599 | 2.0E-64 |
| sp|P46703|ACDP_MYCLE | Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium leprae (strain TN) GN=fadE25 PE=3 SV=1 | 227 | 597 | 7.0E-63 |
| sp|P51174|ACADL_MOUSE | Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadl PE=1 SV=2 | 234 | 599 | 8.0E-62 |
| sp|P15650|ACADL_RAT | Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadl PE=1 SV=1 | 234 | 599 | 3.0E-61 |
| sp|P79274|ACADL_PIG | Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Sus scrofa GN=ACADL PE=2 SV=1 | 234 | 599 | 7.0E-61 |
| sp|Q0NXR6|ACAD8_BOVIN | Isobutyryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACAD8 PE=2 SV=1 | 226 | 599 | 1.0E-60 |
| sp|Q9D7B6|ACAD8_MOUSE | Isobutyryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acad8 PE=1 SV=2 | 205 | 599 | 3.0E-60 |
| sp|Q9H845|ACAD9_HUMAN | Acyl-CoA dehydrogenase family member 9, mitochondrial OS=Homo sapiens GN=ACAD9 PE=1 SV=1 | 233 | 607 | 2.0E-59 |
| sp|Q8JZN5|ACAD9_MOUSE | Acyl-CoA dehydrogenase family member 9, mitochondrial OS=Mus musculus GN=Acad9 PE=1 SV=2 | 233 | 607 | 2.0E-58 |
| sp|P28330|ACADL_HUMAN | Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADL PE=1 SV=2 | 234 | 599 | 3.0E-58 |
| sp|Q9UKU7|ACAD8_HUMAN | Isobutyryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACAD8 PE=1 SV=1 | 226 | 599 | 4.0E-58 |
| sp|Q9VSA3|ACADM_DROME | Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Drosophila melanogaster GN=CG12262 PE=1 SV=1 | 221 | 601 | 5.0E-58 |
| sp|Q60HI0|ACADL_MACFA | Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADL PE=2 SV=1 | 234 | 598 | 6.0E-58 |
| sp|Q2LQP0|CHCOA_SYNAS | Cyclohexane-1-carbonyl-CoA dehydrogenase OS=Syntrophus aciditrophicus (strain SB) GN=SYN_02586 PE=1 SV=1 | 221 | 602 | 1.0E-56 |
| sp|C3UVB0|ACD_DESML | Glutaryl-CoA dehydrogenase OS=Desulfococcus multivorans GN=Acd PE=1 SV=1 | 227 | 595 | 3.0E-56 |
| sp|P41367|ACADM_PIG | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Sus scrofa GN=ACADM PE=1 SV=3 | 227 | 598 | 3.0E-56 |
| sp|Q22347|ACADM_CAEEL | Probable medium-chain specific acyl-CoA dehydrogenase 10, mitochondrial OS=Caenorhabditis elegans GN=acdh-10 PE=2 SV=1 | 211 | 602 | 4.0E-56 |
| sp|A8XNF0|ACAD1_CAEBR | Probable medium-chain specific acyl-CoA dehydrogenase 1, mitochondrial OS=Caenorhabditis briggsae GN=CBG15946 PE=3 SV=1 | 211 | 602 | 1.0E-55 |
| sp|P11310|ACADM_HUMAN | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADM PE=1 SV=1 | 227 | 598 | 1.0E-54 |
| sp|A5A6I0|ACADM_PANTR | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Pan troglodytes GN=ACADM PE=2 SV=1 | 227 | 598 | 2.0E-54 |
| sp|O32176|FADE_BACSU | Probable acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) GN=fadE PE=2 SV=1 | 227 | 599 | 3.0E-54 |
| sp|Q8HXY8|ACADM_MACFA | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADM PE=2 SV=1 | 227 | 598 | 2.0E-53 |
| sp|Q3SZB4|ACADM_BOVIN | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADM PE=2 SV=1 | 211 | 598 | 6.0E-52 |
| sp|P45952|ACADM_MOUSE | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadm PE=1 SV=1 | 227 | 601 | 6.0E-52 |
| sp|Q20772|GCDH_CAEEL | Probable glutaryl-CoA dehydrogenase, mitochondrial OS=Caenorhabditis elegans GN=F54D5.7 PE=1 SV=1 | 227 | 597 | 8.0E-52 |
| sp|A8WP91|ACAD2_CAEBR | Probable medium-chain specific acyl-CoA dehydrogenase 2, mitochondrial OS=Caenorhabditis briggsae GN=CBG00953 PE=3 SV=2 | 227 | 602 | 1.0E-51 |
| sp|P08503|ACADM_RAT | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadm PE=1 SV=1 | 205 | 601 | 3.0E-51 |
| sp|P49748|ACADV_HUMAN | Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADVL PE=1 SV=1 | 227 | 595 | 1.0E-50 |
| sp|Q8HXY7|ACADV_MACFA | Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADVL PE=2 SV=1 | 227 | 595 | 1.0E-49 |
| sp|Q54R47|GCDH_DICDI | Glutaryl-CoA dehydrogenase, mitochondrial OS=Dictyostelium discoideum GN=gcdh PE=3 SV=1 | 227 | 597 | 4.0E-49 |
| sp|P45953|ACADV_RAT | Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadvl PE=1 SV=1 | 262 | 595 | 8.0E-47 |
| sp|P48818|ACADV_BOVIN | Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADVL PE=2 SV=3 | 265 | 595 | 3.0E-46 |
| sp|P50544|ACADV_MOUSE | Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadvl PE=1 SV=3 | 262 | 595 | 8.0E-46 |
| sp|Q96329|ACOX4_ARATH | Acyl-coenzyme A oxidase 4, peroxisomal OS=Arabidopsis thaliana GN=ACX4 PE=1 SV=1 | 227 | 598 | 3.0E-45 |
| sp|Q2KHZ9|GCDH_BOVIN | Glutaryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=GCDH PE=2 SV=1 | 227 | 597 | 2.0E-43 |
| sp|P81140|GCDH_PIG | Glutaryl-CoA dehydrogenase, mitochondrial (Fragment) OS=Sus scrofa GN=GCDH PE=1 SV=1 | 227 | 597 | 3.0E-42 |
| sp|Q92947|GCDH_HUMAN | Glutaryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=GCDH PE=1 SV=1 | 227 | 597 | 3.0E-41 |
| sp|Q0T8F5|CAIA_SHIF8 | Crotonobetainyl-CoA dehydrogenase OS=Shigella flexneri serotype 5b (strain 8401) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-40 |
| sp|Q3Z5W9|CAIA_SHISS | Crotonobetainyl-CoA dehydrogenase OS=Shigella sonnei (strain Ss046) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|P60587|CAIA_SHIFL | Crotonobetainyl-CoA dehydrogenase OS=Shigella flexneri GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|Q32K58|CAIA_SHIDS | Crotonobetainyl-CoA dehydrogenase OS=Shigella dysenteriae serotype 1 (strain Sd197) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|B7LWN0|CAIA_ESCF3 | Crotonobetainyl-CoA dehydrogenase OS=Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|Q1RGF9|CAIA_ECOUT | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain UTI89 / UPEC) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|B1LFX2|CAIA_ECOSM | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain SMS-3-5 / SECEC) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|B6HYZ0|CAIA_ECOSE | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain SE11) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|B7N7R4|CAIA_ECOLU | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|P60584|CAIA_ECOLI | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain K12) GN=caiA PE=1 SV=1 | 251 | 597 | 2.0E-40 |
| sp|B1IRD7|CAIA_ECOLC | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|P60585|CAIA_ECOL6 | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|A1A789|CAIA_ECOK1 | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O1:K1 / APEC GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|A7ZVY9|CAIA_ECOHS | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O9:H4 (strain HS) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|B1XBG4|CAIA_ECODH | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain K12 / DH10B) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|C4ZPW5|CAIA_ECOBW | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain K12 / MC4100 / BW2952) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|B7MNP6|CAIA_ECO81 | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O81 (strain ED1a) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|B7NHE3|CAIA_ECO7I | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O7:K1 (strain IAI39 / ExPEC) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|B5YYD3|CAIA_ECO5E | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O157:H7 (strain EC4115 / EHEC) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|P60586|CAIA_ECO57 | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O157:H7 GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|B7L4G2|CAIA_ECO55 | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain 55989 / EAEC) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|B7MAG2|CAIA_ECO45 | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O45:K1 (strain S88 / ExPEC) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|B7UI85|CAIA_ECO27 | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O127:H6 (strain E2348/69 / EPEC) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|A7ZHD0|CAIA_ECO24 | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O139:H28 (strain E24377A / ETEC) GN=caiA PE=3 SV=1 | 251 | 597 | 2.0E-40 |
| sp|Q0TLV0|CAIA_ECOL5 | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O6:K15:H31 (strain 536 / UPEC) GN=caiA PE=3 SV=1 | 251 | 597 | 3.0E-40 |
| sp|B7M0D6|CAIA_ECO8A | Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O8 (strain IAI1) GN=caiA PE=3 SV=1 | 251 | 597 | 3.0E-40 |
| sp|Q8HXX8|GCDH_MACFA | Glutaryl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=GCDH PE=2 SV=1 | 227 | 597 | 5.0E-40 |
| sp|Q60759|GCDH_MOUSE | Glutaryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Gcdh PE=1 SV=2 | 227 | 597 | 2.0E-39 |
| sp|Q8GB20|CAIA_PROSL | Crotonobetainyl-CoA dehydrogenase OS=Proteus sp. (strain LE138) GN=caiA PE=3 SV=1 | 227 | 597 | 3.0E-39 |
| sp|B4EY23|CAIA_PROMH | Crotonobetainyl-CoA dehydrogenase OS=Proteus mirabilis (strain HI4320) GN=caiA PE=3 SV=1 | 227 | 597 | 3.0E-39 |
| sp|A9MQH5|CAIA_SALAR | Crotonobetainyl-CoA dehydrogenase OS=Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980) GN=caiA PE=3 SV=1 | 251 | 597 | 7.0E-39 |
| sp|Q8ZRX2|CAIA_SALTY | Crotonobetainyl-CoA dehydrogenase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|B4TWR6|CAIA_SALSV | Crotonobetainyl-CoA dehydrogenase OS=Salmonella schwarzengrund (strain CVM19633) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|B5BL57|CAIA_SALPK | Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi A (strain AKU_12601) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|C0Q4L5|CAIA_SALPC | Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi C (strain RKS4594) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|A9MYJ9|CAIA_SALPB | Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|Q5PIN6|CAIA_SALPA | Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi A (strain ATCC 9150 / SARB42) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|B4T6J8|CAIA_SALNS | Crotonobetainyl-CoA dehydrogenase OS=Salmonella newport (strain SL254) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|B4TIH2|CAIA_SALHS | Crotonobetainyl-CoA dehydrogenase OS=Salmonella heidelberg (strain SL476) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|B5RGA6|CAIA_SALG2 | Crotonobetainyl-CoA dehydrogenase OS=Salmonella gallinarum (strain 287/91 / NCTC 13346) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|B5R1R2|CAIA_SALEP | Crotonobetainyl-CoA dehydrogenase OS=Salmonella enteritidis PT4 (strain P125109) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|B5FHG7|CAIA_SALDC | Crotonobetainyl-CoA dehydrogenase OS=Salmonella dublin (strain CT_02021853) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|Q57TI8|CAIA_SALCH | Crotonobetainyl-CoA dehydrogenase OS=Salmonella choleraesuis (strain SC-B67) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|B5F752|CAIA_SALA4 | Crotonobetainyl-CoA dehydrogenase OS=Salmonella agona (strain SL483) GN=caiA PE=3 SV=1 | 251 | 597 | 1.0E-38 |
| sp|Q8Z9L2|CAIA_SALTI | Crotonobetainyl-CoA dehydrogenase OS=Salmonella typhi GN=caiA PE=3 SV=1 | 251 | 597 | 4.0E-38 |
| sp|P34275|IVD_CAEEL | Probable acyl-CoA dehydrogenase 6 OS=Caenorhabditis elegans GN=acdh-6 PE=3 SV=2 | 221 | 595 | 5.0E-38 |
| sp|A8ALR4|CAIA_CITK8 | Crotonobetainyl-CoA dehydrogenase OS=Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) GN=caiA PE=3 SV=1 | 251 | 597 | 6.0E-38 |
| sp|P0A9U8|YDIO_ECOLI | Probable acyl-CoA dehydrogenase YdiO OS=Escherichia coli (strain K12) GN=ydiO PE=3 SV=1 | 254 | 598 | 9.0E-35 |
| sp|P0A9U9|YDIO_ECOL6 | Probable acyl-CoA dehydrogenase YdiO OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) GN=ydiO PE=3 SV=1 | 254 | 598 | 9.0E-35 |
| sp|P0A9V0|YDIO_ECO57 | Probable acyl-CoA dehydrogenase YdiO OS=Escherichia coli O157:H7 GN=ydiO PE=3 SV=1 | 254 | 598 | 9.0E-35 |
| sp|P63430|Y897_MYCBO | Probable acyl-CoA dehydrogenase FadE10 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=fadE10 PE=3 SV=1 | 253 | 598 | 2.0E-31 |
| sp|P9WQF7|Y873_MYCTU | Probable acyl-CoA dehydrogenase FadE10 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=fadE10 PE=1 SV=1 | 253 | 598 | 2.0E-31 |
| sp|P9WQF6|Y873_MYCTO | Probable acyl-CoA dehydrogenase FadE10 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=fadE10 PE=3 SV=1 | 253 | 598 | 2.0E-31 |
| sp|Q9KJE8|BBSG_THAAR | (R)-benzylsuccinyl-CoA dehydrogenase OS=Thauera aromatica GN=bbsG PE=1 SV=1 | 270 | 599 | 1.0E-22 |
| sp|P9WQG3|ACDC_MYCTU | Acyl-CoA dehydrogenase fadE12 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=fadE12 PE=1 SV=1 | 262 | 590 | 6.0E-22 |
| sp|P9WQG2|ACDC_MYCTO | Acyl-CoA dehydrogenase fadE12 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=fadE12 PE=3 SV=1 | 262 | 590 | 6.0E-22 |
| sp|Q7U0Y2|ACDC_MYCBO | Acyl-CoA dehydrogenase fadE12 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=fadE12 PE=3 SV=1 | 262 | 590 | 8.0E-22 |
| sp|P0CO34|IPPK_CRYNJ | Inositol-pentakisphosphate 2-kinase OS=Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) GN=IPK1 PE=3 SV=1 | 1 | 198 | 2.0E-19 |
| sp|P0CO35|IPPK_CRYNB | Inositol-pentakisphosphate 2-kinase OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) GN=IPK1 PE=3 SV=1 | 1 | 198 | 2.0E-19 |
| sp|P33224|AIDB_ECOLI | Putative acyl-CoA dehydrogenase AidB OS=Escherichia coli (strain K12) GN=aidB PE=1 SV=3 | 336 | 602 | 5.0E-18 |
| sp|Q73ZP8|MBTN_MYCPA | Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) GN=mbtN PE=3 SV=1 | 260 | 590 | 2.0E-17 |
| sp|Q1BBA3|MBTN_MYCSS | Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium sp. (strain MCS) GN=mbtN PE=3 SV=1 | 329 | 590 | 2.0E-16 |
| sp|Q8K370|ACD10_MOUSE | Acyl-CoA dehydrogenase family member 10 OS=Mus musculus GN=Acad10 PE=1 SV=1 | 226 | 597 | 8.0E-16 |
| sp|P9WQF9|MBTN_MYCTU | Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=mbtN PE=1 SV=1 | 233 | 603 | 2.0E-15 |
| sp|P9WQF8|MBTN_MYCTO | Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=mbtN PE=3 SV=1 | 233 | 603 | 2.0E-15 |
| sp|P63432|MBTN_MYCBO | Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=mbtN PE=3 SV=1 | 233 | 603 | 2.0E-15 |
| sp|Q6JQN1|ACD10_HUMAN | Acyl-CoA dehydrogenase family member 10 OS=Homo sapiens GN=ACAD10 PE=1 SV=1 | 242 | 597 | 1.0E-14 |
| sp|Q4P4C1|IPPK_USTMA | Inositol-pentakisphosphate 2-kinase OS=Ustilago maydis (strain 521 / FGSC 9021) GN=IPK1 PE=3 SV=2 | 12 | 203 | 2.0E-14 |
| sp|Q5LLW7|DMDC_RUEPO | 3-methylmercaptopropionyl-CoA dehydrogenase OS=Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) GN=dmdC PE=1 SV=1 | 264 | 598 | 7.0E-14 |
| sp|Q9XWZ2|ACD11_CAEEL | Acyl-CoA dehydrogenase family member 11 OS=Caenorhabditis elegans GN=acdh-11 PE=1 SV=1 | 289 | 607 | 6.0E-12 |
| sp|Q8X7R2|FADE_ECO57 | Acyl-coenzyme A dehydrogenase OS=Escherichia coli O157:H7 GN=fadE PE=3 SV=2 | 219 | 566 | 1.0E-11 |
| sp|Q8ZRJ7|FADE_SALTY | Acyl-coenzyme A dehydrogenase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN=fadE PE=2 SV=1 | 219 | 566 | 1.0E-11 |
| sp|Q8Z937|FADE_SALTI | Acyl-coenzyme A dehydrogenase OS=Salmonella typhi GN=fadE PE=3 SV=1 | 219 | 566 | 2.0E-11 |
| sp|Q47146|FADE_ECOLI | Acyl-coenzyme A dehydrogenase OS=Escherichia coli (strain K12) GN=fadE PE=2 SV=2 | 219 | 566 | 2.0E-11 |
| sp|P96608|YDBM_BACSU | Putative acyl-CoA dehydrogenase YdbM OS=Bacillus subtilis (strain 168) GN=ydbM PE=2 SV=1 | 245 | 579 | 3.0E-11 |
| sp|Q8ZBY6|FADE_YERPE | Acyl-coenzyme A dehydrogenase OS=Yersinia pestis GN=fadE PE=3 SV=1 | 219 | 564 | 6.0E-11 |
| sp|Q5ZHT1|ACD11_CHICK | Acyl-CoA dehydrogenase family member 11 OS=Gallus gallus GN=ACAD11 PE=2 SV=1 | 320 | 597 | 6.0E-11 |
| sp|Q8RWZ3|IBR3_ARATH | Probable acyl-CoA dehydrogenase IBR3 OS=Arabidopsis thaliana GN=IBR3 PE=1 SV=1 | 272 | 597 | 7.0E-10 |
| sp|B3DMA2|ACD11_RAT | Acyl-CoA dehydrogenase family member 11 OS=Rattus norvegicus GN=Acad11 PE=1 SV=1 | 320 | 597 | 7.0E-09 |
| sp|Q80XL6|ACD11_MOUSE | Acyl-CoA dehydrogenase family member 11 OS=Mus musculus GN=Acad11 PE=1 SV=2 | 320 | 597 | 3.0E-08 |
| sp|Q5R778|ACD11_PONAB | Acyl-CoA dehydrogenase family member 11 OS=Pongo abelii GN=ACAD11 PE=2 SV=2 | 320 | 591 | 1.0E-07 |
| sp|Q709F0|ACD11_HUMAN | Acyl-CoA dehydrogenase family member 11 OS=Homo sapiens GN=ACAD11 PE=1 SV=2 | 320 | 591 | 1.0E-07 |
| sp|P54998|SOXC_RHOSG | Dibenzothiophene desulfurization enzyme C OS=Rhodococcus sp. (strain IGTS8) GN=soxC PE=1 SV=1 | 250 | 583 | 3.0E-07 |
| sp|Q7XQZ6|IPK1_ORYSJ | Inositol-pentakisphosphate 2-kinase IPK1 OS=Oryza sativa subsp. japonica GN=IPK1 PE=2 SV=1 | 1 | 203 | 2.0E-06 |
| sp|B8AVX5|IPK1_ORYSI | Inositol-pentakisphosphate 2-kinase IPK1 OS=Oryza sativa subsp. indica GN=IPK1 PE=3 SV=1 | 1 | 203 | 2.0E-06 |
| sp|O64894|ACOX2_CUCMA | Acyl-coenzyme A oxidase, peroxisomal OS=Cucurbita maxima GN=Acx PE=1 SV=1 | 295 | 590 | 5.0E-06 |
| sp|P0CZ23|ACOX3_ARATH | Acyl-coenzyme A oxidase 3, peroxisomal OS=Arabidopsis thaliana GN=ACX3 PE=1 SV=1 | 282 | 493 | 7.0E-06 |
| GO Term | Description | Terminal node |
|---|---|---|
| GO:0016627 | oxidoreductase activity, acting on the CH-CH group of donors | Yes |
| GO:0035299 | inositol pentakisphosphate 2-kinase activity | Yes |
| GO:0050660 | flavin adenine dinucleotide binding | Yes |
| GO:0005524 | ATP binding | Yes |
| GO:0097367 | carbohydrate derivative binding | No |
| GO:0036094 | small molecule binding | No |
| GO:0030554 | adenyl nucleotide binding | No |
| GO:1901363 | heterocyclic compound binding | No |
| GO:0005488 | binding | No |
| GO:0043167 | ion binding | No |
| GO:0016773 | phosphotransferase activity, alcohol group as acceptor | No |
| GO:0032559 | adenyl ribonucleotide binding | No |
| GO:0043168 | anion binding | No |
| GO:0016301 | kinase activity | No |
| GO:0016772 | transferase activity, transferring phosphorus-containing groups | No |
| GO:0097159 | organic cyclic compound binding | No |
| GO:0017076 | purine nucleotide binding | No |
| GO:0035639 | purine ribonucleoside triphosphate binding | No |
| GO:0016740 | transferase activity | No |
| GO:0003674 | molecular_function | No |
| GO:1901265 | nucleoside phosphate binding | No |
| GO:0032553 | ribonucleotide binding | No |
| GO:0003824 | catalytic activity | No |
| GO:0016491 | oxidoreductase activity | No |
| GO:0032555 | purine ribonucleotide binding | No |
| GO:0000166 | nucleotide binding | No |
| SignalP signal predicted | Location (based on Ymax) |
D score (significance: > 0.45) |
|---|---|---|
| No | 1 - 13 | 0.45 |
| Type of sequence | Sequence |
|---|---|
| Locus | Download genbank file of locus
The gene with 5 kb flanks (if sufficient flanking sequence is available). For use in cloning design programs. NOTE: features (genes or exons) that are only partially contained within the sequence are completely excluded. |
| Protein | >AgabiH97|056320 MHSHMRSSKDCKYANKYCPLDLFSGNPHRVQQAIDDLWDAWERSDGEVNNLKIFSRGKAVRPGQIVRLLHEDFIT SVSPDRIQEVFKKALCDTLLQSPILSIISRLQRTLDVLDIEGLSKLWREAQLESLSDEQIQTSSPPLTYLLSATF KDCSIIARLGLLKPGNHSEIQEEQIRVIDLDPKSLNRLPRWEELDREIVMSYVPAERKMPALQKRAISLYNSEVS GLTDEELEFRNAVVDFAQKEVAPRAAEIDRTNISPMDLWEKLGSMGLLGITVDQKYNGLNLGYLHHTLAMEALSE ASGSVALSYGAHSNLCVNQIHRHGTEAQKEKYLKDLVDGTKVGSLAMSETGSGSDVVSMRLKAEKVQGGWKLNGN KFWITNGPVASTLVVYAKTAPELGSKGITTFVIERGFEGFSTSQKLDKFGMRGSDTCELVFEDCVVPEENVLGQV NKGAAVLMSGLDLERVVLSGGPLGLMQAAFDYAVEYIHDRKQFGQPVGTFQLMQAKIADMYTKLNASRSYVYSVA RACDRGKVSRKDCAGAIMYSTEKAVEVALEGMQCLGGNGYINDYPMGRILRDSRLYTVGAGTQEIRRMLIGREFN EHDYCIL* |
| Coding | >AgabiH97|056320 ATGCATAGTCATATGCGTAGCAGTAAAGATTGCAAGTATGCCAACAAGTACTGCCCCCTCGACTTGTTCTCTGGA AACCCCCATCGTGTTCAACAAGCCATCGACGACTTATGGGACGCCTGGGAGCGAAGTGACGGCGAGGTCAACAAT CTAAAAATATTTTCACGCGGGAAGGCAGTTAGGCCAGGCCAGATTGTACGCTTGTTGCACGAAGATTTCATAACG TCCGTATCTCCTGATAGGATACAAGAGGTTTTCAAAAAGGCGTTGTGTGACACCCTTCTGCAATCGCCCATTCTC AGCATCATCTCGAGGCTCCAGAGGACTTTGGATGTTTTGGATATCGAGGGTCTATCGAAATTATGGCGTGAAGCT CAACTTGAGTCTCTCTCTGACGAGCAGATACAGACTTCGTCACCGCCTTTGACGTATCTACTTTCGGCAACATTC AAGGACTGCTCAATCATTGCCAGGCTGGGGTTGCTGAAACCCGGGAACCATTCTGAAATTCAGGAAGAACAAATA CGTGTGATTGACTTGGACCCCAAGAGTCTGAACCGGCTGCCGCGCTGGGAAGAGTTGGATAGGGAGATTGTGATG AGTTATGTACCTGCTGAGAGGAAGATGCCCGCTCTCCAGAAACGCGCCATTTCTCTGTACAATTCCGAAGTCTCT GGTCTCACGGACGAAGAACTCGAGTTTCGTAATGCCGTCGTCGACTTTGCACAGAAAGAAGTAGCACCGAGGGCA GCCGAGATAGATAGGACGAATATCTCTCCCATGGACCTCTGGGAGAAGCTCGGTTCTATGGGTCTCCTCGGTATA ACCGTAGATCAAAAATATAATGGCTTAAATCTTGGATATCTTCACCACACGCTTGCAATGGAAGCTCTATCTGAG GCCTCGGGATCTGTAGCACTGTCCTACGGAGCCCATTCCAACCTCTGTGTGAACCAGATTCACCGACACGGGACG GAAGCACAAAAGGAGAAATACCTCAAGGATCTTGTTGACGGAACCAAAGTCGGAAGCTTGGCAATGAGTGAAACT GGAAGTGGAAGTGACGTGGTCAGTATGCGTTTAAAGGCGGAAAAGGTTCAAGGCGGATGGAAGCTGAATGGTAAC AAATTTTGGATCACAAATGGGCCCGTCGCCTCCACGCTGGTCGTATATGCCAAAACGGCTCCAGAATTGGGGTCT AAAGGGATCACAACTTTCGTTATTGAGCGTGGTTTCGAGGGTTTTTCCACCAGCCAGAAGCTTGATAAATTTGGA ATGAGAGGAAGTGATACCTGTGAACTTGTCTTCGAGGATTGCGTAGTTCCTGAGGAGAATGTCCTCGGCCAGGTC AACAAGGGTGCTGCCGTTTTGATGTCAGGATTAGATCTTGAACGAGTGGTTCTCAGCGGCGGTCCTTTGGGGTTA ATGCAGGCGGCGTTTGACTATGCCGTGGAGTATATCCACGATAGGAAGCAGTTTGGTCAACCCGTTGGTACATTC CAGTTAATGCAAGCCAAAATTGCCGACATGTATACGAAGCTGAATGCTAGTCGGTCGTATGTATATTCAGTAGCC CGTGCGTGCGATCGAGGTAAAGTTAGTCGCAAAGATTGTGCTGGCGCTATCATGTATTCGACGGAGAAAGCCGTC GAAGTTGCTCTGGAAGGTATGCAGTGCCTTGGAGGTAATGGCTACATCAACGATTACCCAATGGGTCGTATTCTC CGGGATTCTCGCTTATATACCGTCGGAGCCGGCACTCAAGAAATTCGGCGAATGCTAATTGGAAGGGAATTCAAC GAGCACGACTATTGTATTTTATAG |
| Transcript | >AgabiH97|056320 ATGCATAGTCATATGCGTAGCAGTAAAGATTGCAAGTATGCCAACAAGTACTGCCCCCTCGACTTGTTCTCTGGA AACCCCCATCGTGTTCAACAAGCCATCGACGACTTATGGGACGCCTGGGAGCGAAGTGACGGCGAGGTCAACAAT CTAAAAATATTTTCACGCGGGAAGGCAGTTAGGCCAGGCCAGATTGTACGCTTGTTGCACGAAGATTTCATAACG TCCGTATCTCCTGATAGGATACAAGAGGTTTTCAAAAAGGCGTTGTGTGACACCCTTCTGCAATCGCCCATTCTC AGCATCATCTCGAGGCTCCAGAGGACTTTGGATGTTTTGGATATCGAGGGTCTATCGAAATTATGGCGTGAAGCT CAACTTGAGTCTCTCTCTGACGAGCAGATACAGACTTCGTCACCGCCTTTGACGTATCTACTTTCGGCAACATTC AAGGACTGCTCAATCATTGCCAGGCTGGGGTTGCTGAAACCCGGGAACCATTCTGAAATTCAGGAAGAACAAATA CGTGTGATTGACTTGGACCCCAAGAGTCTGAACCGGCTGCCGCGCTGGGAAGAGTTGGATAGGGAGATTGTGATG AGTTATGTACCTGCTGAGAGGAAGATGCCCGCTCTCCAGAAACGCGCCATTTCTCTGTACAATTCCGAAGTCTCT GGTCTCACGGACGAAGAACTCGAGTTTCGTAATGCCGTCGTCGACTTTGCACAGAAAGAAGTAGCACCGAGGGCA GCCGAGATAGATAGGACGAATATCTCTCCCATGGACCTCTGGGAGAAGCTCGGTTCTATGGGTCTCCTCGGTATA ACCGTAGATCAAAAATATAATGGCTTAAATCTTGGATATCTTCACCACACGCTTGCAATGGAAGCTCTATCTGAG GCCTCGGGATCTGTAGCACTGTCCTACGGAGCCCATTCCAACCTCTGTGTGAACCAGATTCACCGACACGGGACG GAAGCACAAAAGGAGAAATACCTCAAGGATCTTGTTGACGGAACCAAAGTCGGAAGCTTGGCAATGAGTGAAACT GGAAGTGGAAGTGACGTGGTCAGTATGCGTTTAAAGGCGGAAAAGGTTCAAGGCGGATGGAAGCTGAATGGTAAC AAATTTTGGATCACAAATGGGCCCGTCGCCTCCACGCTGGTCGTATATGCCAAAACGGCTCCAGAATTGGGGTCT AAAGGGATCACAACTTTCGTTATTGAGCGTGGTTTCGAGGGTTTTTCCACCAGCCAGAAGCTTGATAAATTTGGA ATGAGAGGAAGTGATACCTGTGAACTTGTCTTCGAGGATTGCGTAGTTCCTGAGGAGAATGTCCTCGGCCAGGTC AACAAGGGTGCTGCCGTTTTGATGTCAGGATTAGATCTTGAACGAGTGGTTCTCAGCGGCGGTCCTTTGGGGTTA ATGCAGGCGGCGTTTGACTATGCCGTGGAGTATATCCACGATAGGAAGCAGTTTGGTCAACCCGTTGGTACATTC CAGTTAATGCAAGCCAAAATTGCCGACATGTATACGAAGCTGAATGCTAGTCGGTCGTATGTATATTCAGTAGCC CGTGCGTGCGATCGAGGTAAAGTTAGTCGCAAAGATTGTGCTGGCGCTATCATGTATTCGACGGAGAAAGCCGTC GAAGTTGCTCTGGAAGGTATGCAGTGCCTTGGAGGTAATGGCTACATCAACGATTACCCAATGGGTCGTATTCTC CGGGATTCTCGCTTATATACCGTCGGAGCCGGCACTCAAGAAATTCGGCGAATGCTAATTGGAAGGGAATTCAAC GAGCACGACTATTGTATTTTATAG |
| Gene | >AgabiH97|056320 ATGCATAGTCATATGCGTAGCAGTAAAGATTGCAAGTATGCCAACAAGTACTGCCCCCTCGACTTGTTCTCTGGA AACCCCCATCGTGTTCAACAAGCCATCGACGACTTATGGGACGCCTGGGAGCGAAGTGACGGCGAGGTCAACAAT CTAAAAATATTTTCACGCGGGAAGGCAGTTAGGCCAGGCCAGGTACGCTTGTTTCTGCACATGCGATACTGTAGC TTAAGCTAAAGGCAATCGAGATTGTACGCTTGTTGCACGAAGATTTCATAACGTCCGTATCTCCTGATAGGATAC AAGAGGTTTTCAAAAAGGCGTTGTGTGACACCCTTCTGCAATCGCCCATTCTCAGCATCATCTCGAGGCTCCAGA GGACTTTGGATGTTTTGGATATCGAGGGTCTATCGAAATTATGGCGTGAAGCTCAACTTGAGTCTCTCTCTGACG AGCAGATACAGGTACCTCCGCTCGGCGTTTCGCAATCGGAGCCCGGAATGACGGATTGGGTAGACTTCGTCACCG CCTTTGAGTCTGTTGAGATGAAGGAACTGGACCATGACCAGCCAAGGACAAGCAATCTTCGATATTACATTTTAG CGTATCTACTTTCGGCAACATTCAAGGACTGCTCAATCATTGCCAGGCTGGGGTTGCTGAAACCCGGGAACCATT CTGAAATTCAGGAAGAACAAATACGTGTGATTGACTTGGACCCCAAGAGTCTGAACCGGCTGCCGCGCTGGGAAG AGTTGGATAGGGAGATTGTGATGAGTTATGTACCTGCTGAGAGGAAGATGTGCGTTGACGAGAACATAGTACCAT CACGTGTAGCCTCCGGCAATGGTCCGGAGAGTTAAGTAGGACCGTCTTGAGTCGAATTTTGACCTTGCACACACA TGGCTTCTCTCCGAACCTTGCTTCGTCCTCTGAACCGTCTATCCATCAGGCCCGCTCTCCAGAAACGCGCCATTT CTCTGTACAATTCCGAAGTCTCTGGTCTCACGGACGAAGAACTCGAGGTTCGTCGTTTCGACGGCAAATTCTGAC ATCCTCGTTGACGAGAGCTACTTAGTTTCGTAATGCCGTCGTCGACTTTGCACAGAAAGAAGTAGCACCGAGGGC AGCCGAGATAGATAGGACGAATATCTCTCCCATGGTGTGACCTTCGACATATCAGAGTAATATTGTGCTTACTCG CGAACTTCCCTAGGACCTCTGGGAGAAGCTCGGTTCTATGGGTCTCCTCGGTATAACCGTAGATCAAAAATATAA TGGCTTAAATCTTGGATATCTTCACCACACGCTTGCAATGGAAGCTCTATCTGAGGCCTCGGGATCTGTAGCACT GTCCTACGGAGCCCATTCCAACCTCTGTGTGAACCAGATTCACCGACACGGGACGGAAGCACAAAAGGAGAAATA CCTCAAGGATCTTGTTGACGGAACCAAAGTCGGAAGCTTGGCAATGAGTGAAACTGGAAGTGGAAGTGACGTGGT CAGTATGCGTTTAAAGGCGGAAAAGGTTCAAGGCGGATGGAAGCTGAATGGTAACAAATTTTGGTGAGTTGTATA CTCGATCCATTCTCTCGCACGGGTACCTATGTGCTGATAGGAGGGCTTAAAGGATCACAAATGGGCCCGTCGCCT CCACGCTGGTCGTATATGCCAAAACGGCTCCAGAATTGGGGTCTAAAGGGATCACAACTTTCGTTATTGAGCGTG GTTTCGAGGGTTTTTCCACCAGCCAGAAGCTTGATAAATTTGGAATGAGAGGAAGTGATACCTGTGAACTTGTCT TCGAGGATTGCGTAGTTCCTGAGGGTATGTTTGTTTTTGGTTCCTCGAGTCAAATTTACGATCCAATGCTACTAT AGAGAATGTCCTCGGCCAGGTCAACAAGGGTGCTGCCGTTTTGATGTCAGGATTAGATCTTGAACGAGTGGTTCT CAGCGGCGGTCCTTTGGGGTTTGTTGATTACATCGATCTTGCTGGTTGTAACGGCGGTTGATCACTAAGTTAGGT TAATGCAGGCGGCGTTTGACTATGCCGTGGAGTATATCCACGATAGGAAGCAGTTTGGTCAACCCGTTGGTACAT TCCAGTTAATGCAAGGCGAGTCATCCTTATTAGATTCATTTTATTCTCTTTTAACGCTCTTGTAGCCAAAATTGC CGACATGTATACGAAGCTGAATGCTAGTCGGTCGTATGTATATTCAGTAGCCCGTGCGTGCGATCGAGGTAAAGT TAGTCGCAAAGTAAGTCATGCGTTTCCTACTTCAAGCAATCTCCTGCTTGGTTTGTGTAGCGGCACTGATAATTT GCGGTTATAGGATTGTGCTGGCGCTATCATGTATTCGACGGAGAAAGCCGTCGAAGTTGCTCTGGAAGGTATGCA GTGCCTTGGAGGTAATGGCTACATCAACGGTTAGTACATCTATGAGATCTGGCCTAAATCTTGCCTAAGTTGTTG CATCTGCTCAGATTACCCAATGGGTCGTATTCTCCGGGATTCTCGCTTATATACCGTCGGAGCCGGCACTCAAGA AATTCGGCGAATGCTAATTGGAAGGGAATTCAACGAGCAGTTTAAGGCATGAAGCGGAATGTTATGTGCTTTTGG CAAACTATCGAACGAACTGTCAAAAGAGTTTGTTAGCGAGTGAGAACTCGTCTTTCATATACTTTGTGGCTGGCC TGTCCACACACTAATTTTGCTTTAGCTATTGTATTTTATAG |