Fungal Genomics

at Utrecht University

General Properties

Protein IDAgabiH97|047910
Gene name
Locationscaffold_2:2331702..2333671
Strand+
Gene length (bp)1969
Transcript length (bp)1263
Coding sequence length (bp)1263
Protein length (aa) 421

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PFAM Domains

PFAM Domain ID Short name Long name E-value Start End
PF02771 Acyl-CoA_dh_N Acyl-CoA dehydrogenase, N-terminal domain 2.1E-27 46 157
PF00441 Acyl-CoA_dh_1 Acyl-CoA dehydrogenase, C-terminal domain 1.3E-26 265 412
PF02770 Acyl-CoA_dh_M Acyl-CoA dehydrogenase, middle domain 1.2E-19 161 253
PF08028 Acyl-CoA_dh_2 Acyl-CoA dehydrogenase, C-terminal domain 1.1E-07 281 401

Swissprot hits

[Show all]
Swissprot ID Swissprot Description Start End E-value
sp|Q8HXX8|GCDH_MACFA Glutaryl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=GCDH PE=2 SV=1 10 418 0.0E+00
sp|Q92947|GCDH_HUMAN Glutaryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=GCDH PE=1 SV=1 17 418 0.0E+00
sp|P81140|GCDH_PIG Glutaryl-CoA dehydrogenase, mitochondrial (Fragment) OS=Sus scrofa GN=GCDH PE=1 SV=1 21 420 0.0E+00
sp|Q2KHZ9|GCDH_BOVIN Glutaryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=GCDH PE=2 SV=1 24 418 2.0E-179
sp|Q60759|GCDH_MOUSE Glutaryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Gcdh PE=1 SV=2 24 419 1.0E-177
[Show all]
[Show less]
Swissprot ID Swissprot Description Start End E-value
sp|Q8HXX8|GCDH_MACFA Glutaryl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=GCDH PE=2 SV=1 10 418 0.0E+00
sp|Q92947|GCDH_HUMAN Glutaryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=GCDH PE=1 SV=1 17 418 0.0E+00
sp|P81140|GCDH_PIG Glutaryl-CoA dehydrogenase, mitochondrial (Fragment) OS=Sus scrofa GN=GCDH PE=1 SV=1 21 420 0.0E+00
sp|Q2KHZ9|GCDH_BOVIN Glutaryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=GCDH PE=2 SV=1 24 418 2.0E-179
sp|Q60759|GCDH_MOUSE Glutaryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Gcdh PE=1 SV=2 24 419 1.0E-177
sp|Q20772|GCDH_CAEEL Probable glutaryl-CoA dehydrogenase, mitochondrial OS=Caenorhabditis elegans GN=F54D5.7 PE=1 SV=1 23 419 6.0E-165
sp|Q54R47|GCDH_DICDI Glutaryl-CoA dehydrogenase, mitochondrial OS=Dictyostelium discoideum GN=gcdh PE=3 SV=1 32 418 3.0E-164
sp|Q96329|ACOX4_ARATH Acyl-coenzyme A oxidase 4, peroxisomal OS=Arabidopsis thaliana GN=ACX4 PE=1 SV=1 37 418 6.0E-76
sp|P45857|ACDB_BACSU Acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) GN=mmgC PE=2 SV=3 44 410 2.0E-61
sp|Q06319|ACDS_MEGEL Acyl-CoA dehydrogenase, short-chain specific OS=Megasphaera elsdenii PE=1 SV=1 56 412 2.0E-56
sp|P45867|ACDA_BACSU Acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) GN=acdA PE=2 SV=1 45 414 6.0E-54
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 41 412 5.0E-52
sp|O34421|ACDC_BACSU Probable acyl-CoA dehydrogenase YngJ OS=Bacillus subtilis (strain 168) GN=yngJ PE=3 SV=1 39 412 5.0E-50
sp|Q9JHI5|IVD_MOUSE Isovaleryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Ivd PE=1 SV=1 18 413 5.0E-48
sp|Q5RBD5|IVD_PONAB Isovaleryl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=IVD PE=2 SV=1 45 413 4.0E-47
sp|Q75IM9|IVD_ORYSJ Isovaleryl-CoA dehydrogenase, mitochondrial OS=Oryza sativa subsp. japonica GN=Os05g0125500 PE=2 SV=2 52 412 6.0E-47
sp|Q9SWG0|IVD_ARATH Isovaleryl-CoA dehydrogenase, mitochondrial OS=Arabidopsis thaliana GN=IVD PE=1 SV=2 49 412 6.0E-47
sp|P26440|IVD_HUMAN Isovaleryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=IVD PE=1 SV=1 45 413 8.0E-47
sp|O32176|FADE_BACSU Probable acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) GN=fadE PE=2 SV=1 37 418 9.0E-47
sp|Q9FS88|MBCD_SOLTU 2-methylacyl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum GN=2MBCD PE=1 SV=2 52 412 4.0E-46
sp|P12007|IVD_RAT Isovaleryl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Ivd PE=1 SV=2 16 413 1.0E-45
sp|Q5EAD4|ACDSB_BOVIN Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADSB PE=2 SV=1 21 413 3.0E-44
sp|Q3SZI8|IVD_BOVIN Isovaleryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=IVD PE=2 SV=1 45 413 3.0E-44
sp|Q54RR5|ACDSB_DICDI Probable short/branched chain specific acyl-CoA dehydrogenase OS=Dictyostelium discoideum GN=acadsb PE=3 SV=1 17 413 7.0E-44
sp|Q9FS87|IVD_SOLTU Isovaleryl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum GN=IVD PE=1 SV=2 52 412 5.0E-43
sp|Q07417|ACADS_MOUSE Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acads PE=1 SV=2 52 409 7.0E-43
sp|P15651|ACADS_RAT Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acads PE=1 SV=2 52 409 4.0E-42
sp|C3UVB0|ACD_DESML Glutaryl-CoA dehydrogenase OS=Desulfococcus multivorans GN=Acd PE=1 SV=1 41 408 5.0E-42
sp|Q5RAS0|ACADS_PONAB Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=ACADS PE=2 SV=1 55 408 5.0E-42
sp|Q9DBL1|ACDSB_MOUSE Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadsb PE=1 SV=1 9 412 3.0E-41
sp|P16219|ACADS_HUMAN Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADS PE=1 SV=1 55 408 3.0E-41
sp|G3KIM8|ACRC_CLOPR Acryloyl-CoA reductase (NADH) OS=Clostridium propionicum GN=acrC PE=1 SV=1 32 412 4.0E-41
sp|P70584|ACDSB_RAT Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadsb PE=1 SV=1 9 412 3.0E-40
sp|P45954|ACDSB_HUMAN Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADSB PE=1 SV=1 9 412 4.0E-40
sp|Q5RF40|ACDSB_PONAB Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=ACADSB PE=2 SV=1 9 412 4.0E-40
sp|Q9VSA3|ACADM_DROME Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Drosophila melanogaster GN=CG12262 PE=1 SV=1 16 410 4.0E-39
sp|P49748|ACADV_HUMAN Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADVL PE=1 SV=1 82 408 9.0E-39
sp|Q8JZN5|ACAD9_MOUSE Acyl-CoA dehydrogenase family member 9, mitochondrial OS=Mus musculus GN=Acad9 PE=1 SV=2 55 408 4.0E-38
sp|Q8HXY7|ACADV_MACFA Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADVL PE=2 SV=1 82 408 1.0E-37
sp|Q3ZBF6|ACADS_BOVIN Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADS PE=1 SV=1 52 409 2.0E-37
sp|P48818|ACADV_BOVIN Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADVL PE=2 SV=3 73 408 2.0E-37
sp|A8XNF0|ACAD1_CAEBR Probable medium-chain specific acyl-CoA dehydrogenase 1, mitochondrial OS=Caenorhabditis briggsae GN=CBG15946 PE=3 SV=1 45 412 1.0E-36
sp|A8WP91|ACAD2_CAEBR Probable medium-chain specific acyl-CoA dehydrogenase 2, mitochondrial OS=Caenorhabditis briggsae GN=CBG00953 PE=3 SV=2 41 412 3.0E-36
sp|Q22347|ACADM_CAEEL Probable medium-chain specific acyl-CoA dehydrogenase 10, mitochondrial OS=Caenorhabditis elegans GN=acdh-10 PE=2 SV=1 45 412 7.0E-36
sp|P79273|ACADS_PIG Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Sus scrofa GN=ACADS PE=2 SV=1 52 409 8.0E-36
sp|P79274|ACADL_PIG Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Sus scrofa GN=ACADL PE=2 SV=1 45 413 5.0E-35
sp|Q8HXY8|ACADM_MACFA Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADM PE=2 SV=1 25 410 1.0E-34
sp|Q2LQN9|CH1CO_SYNAS Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase OS=Syntrophus aciditrophicus (strain SB) GN=SYN_02587 PE=1 SV=1 43 412 1.0E-34
sp|Q9H845|ACAD9_HUMAN Acyl-CoA dehydrogenase family member 9, mitochondrial OS=Homo sapiens GN=ACAD9 PE=1 SV=1 69 403 5.0E-34
sp|Q54IM8|ACAD8_DICDI Isobutyryl-CoA dehydrogenase, mitochondrial OS=Dictyostelium discoideum GN=acad8 PE=3 SV=1 45 413 6.0E-34
sp|P50544|ACADV_MOUSE Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadvl PE=1 SV=3 78 408 8.0E-34
sp|P45953|ACADV_RAT Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadvl PE=1 SV=1 73 408 8.0E-34
sp|P51174|ACADL_MOUSE Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadl PE=1 SV=2 45 414 4.0E-33
sp|P41367|ACADM_PIG Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Sus scrofa GN=ACADM PE=1 SV=3 44 410 5.0E-33
sp|P15650|ACADL_RAT Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadl PE=1 SV=1 45 413 2.0E-32
sp|Q60HI0|ACADL_MACFA Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADL PE=2 SV=1 45 413 2.0E-32
sp|P11310|ACADM_HUMAN Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADM PE=1 SV=1 25 414 2.0E-32
sp|A5A6I0|ACADM_PANTR Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Pan troglodytes GN=ACADM PE=2 SV=1 25 414 4.0E-32
sp|P28330|ACADL_HUMAN Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADL PE=1 SV=2 45 413 4.0E-32
sp|P9WQG1|ACDP_MYCTU Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=fadE25 PE=1 SV=1 98 412 1.0E-31
sp|P9WQG0|ACDP_MYCTO Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=fadE25 PE=3 SV=1 98 412 1.0E-31
sp|P63428|ACDP_MYCBO Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=fadE25 PE=3 SV=1 98 412 1.0E-31
sp|P46703|ACDP_MYCLE Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium leprae (strain TN) GN=fadE25 PE=3 SV=1 37 412 2.0E-30
sp|Q3SZB4|ACADM_BOVIN Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADM PE=2 SV=1 44 410 3.0E-30
sp|P45952|ACADM_MOUSE Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadm PE=1 SV=1 36 410 4.0E-30
sp|P08503|ACADM_RAT Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadm PE=1 SV=1 25 410 5.0E-30
sp|Q9UKU7|ACAD8_HUMAN Isobutyryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACAD8 PE=1 SV=1 45 412 3.0E-28
sp|Q2LQP0|CHCOA_SYNAS Cyclohexane-1-carbonyl-CoA dehydrogenase OS=Syntrophus aciditrophicus (strain SB) GN=SYN_02586 PE=1 SV=1 136 414 5.0E-28
sp|Q0NXR6|ACAD8_BOVIN Isobutyryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACAD8 PE=2 SV=1 45 412 3.0E-26
sp|Q9D7B6|ACAD8_MOUSE Isobutyryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acad8 PE=1 SV=2 45 410 6.0E-25
sp|P63430|Y897_MYCBO Probable acyl-CoA dehydrogenase FadE10 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=fadE10 PE=3 SV=1 82 414 2.0E-24
sp|P9WQF7|Y873_MYCTU Probable acyl-CoA dehydrogenase FadE10 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=fadE10 PE=1 SV=1 82 414 2.0E-24
sp|P9WQF6|Y873_MYCTO Probable acyl-CoA dehydrogenase FadE10 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=fadE10 PE=3 SV=1 82 414 2.0E-24
sp|Q9KJE8|BBSG_THAAR (R)-benzylsuccinyl-CoA dehydrogenase OS=Thauera aromatica GN=bbsG PE=1 SV=1 42 412 5.0E-22
sp|P34275|IVD_CAEEL Probable acyl-CoA dehydrogenase 6 OS=Caenorhabditis elegans GN=acdh-6 PE=3 SV=2 49 317 6.0E-18
sp|P9WQG3|ACDC_MYCTU Acyl-CoA dehydrogenase fadE12 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=fadE12 PE=1 SV=1 52 329 1.0E-17
sp|P9WQG2|ACDC_MYCTO Acyl-CoA dehydrogenase fadE12 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=fadE12 PE=3 SV=1 52 329 1.0E-17
sp|Q7U0Y2|ACDC_MYCBO Acyl-CoA dehydrogenase fadE12 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=fadE12 PE=3 SV=1 52 329 1.0E-17
sp|Q8GB20|CAIA_PROSL Crotonobetainyl-CoA dehydrogenase OS=Proteus sp. (strain LE138) GN=caiA PE=3 SV=1 141 412 5.0E-14
sp|B4EY23|CAIA_PROMH Crotonobetainyl-CoA dehydrogenase OS=Proteus mirabilis (strain HI4320) GN=caiA PE=3 SV=1 141 412 5.0E-14
sp|Q0T8F5|CAIA_SHIF8 Crotonobetainyl-CoA dehydrogenase OS=Shigella flexneri serotype 5b (strain 8401) GN=caiA PE=3 SV=1 141 412 2.0E-13
sp|A9MQH5|CAIA_SALAR Crotonobetainyl-CoA dehydrogenase OS=Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980) GN=caiA PE=3 SV=1 141 412 3.0E-13
sp|Q8ZRX2|CAIA_SALTY Crotonobetainyl-CoA dehydrogenase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|B4TWR6|CAIA_SALSV Crotonobetainyl-CoA dehydrogenase OS=Salmonella schwarzengrund (strain CVM19633) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|B5BL57|CAIA_SALPK Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi A (strain AKU_12601) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|C0Q4L5|CAIA_SALPC Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi C (strain RKS4594) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|A9MYJ9|CAIA_SALPB Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|Q5PIN6|CAIA_SALPA Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi A (strain ATCC 9150 / SARB42) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|B4T6J8|CAIA_SALNS Crotonobetainyl-CoA dehydrogenase OS=Salmonella newport (strain SL254) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|B4TIH2|CAIA_SALHS Crotonobetainyl-CoA dehydrogenase OS=Salmonella heidelberg (strain SL476) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|B5RGA6|CAIA_SALG2 Crotonobetainyl-CoA dehydrogenase OS=Salmonella gallinarum (strain 287/91 / NCTC 13346) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|B5R1R2|CAIA_SALEP Crotonobetainyl-CoA dehydrogenase OS=Salmonella enteritidis PT4 (strain P125109) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|B5FHG7|CAIA_SALDC Crotonobetainyl-CoA dehydrogenase OS=Salmonella dublin (strain CT_02021853) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|Q57TI8|CAIA_SALCH Crotonobetainyl-CoA dehydrogenase OS=Salmonella choleraesuis (strain SC-B67) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|B5F752|CAIA_SALA4 Crotonobetainyl-CoA dehydrogenase OS=Salmonella agona (strain SL483) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|Q8Z9L2|CAIA_SALTI Crotonobetainyl-CoA dehydrogenase OS=Salmonella typhi GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|A8ALR4|CAIA_CITK8 Crotonobetainyl-CoA dehydrogenase OS=Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) GN=caiA PE=3 SV=1 141 412 6.0E-13
sp|Q3Z5W9|CAIA_SHISS Crotonobetainyl-CoA dehydrogenase OS=Shigella sonnei (strain Ss046) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|P60587|CAIA_SHIFL Crotonobetainyl-CoA dehydrogenase OS=Shigella flexneri GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|Q32K58|CAIA_SHIDS Crotonobetainyl-CoA dehydrogenase OS=Shigella dysenteriae serotype 1 (strain Sd197) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|B7LWN0|CAIA_ESCF3 Crotonobetainyl-CoA dehydrogenase OS=Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|Q1RGF9|CAIA_ECOUT Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain UTI89 / UPEC) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|B1LFX2|CAIA_ECOSM Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain SMS-3-5 / SECEC) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|B6HYZ0|CAIA_ECOSE Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain SE11) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|B7N7R4|CAIA_ECOLU Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|P60584|CAIA_ECOLI Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain K12) GN=caiA PE=1 SV=1 141 412 8.0E-13
sp|B1IRD7|CAIA_ECOLC Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|P60585|CAIA_ECOL6 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|A1A789|CAIA_ECOK1 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O1:K1 / APEC GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|A7ZVY9|CAIA_ECOHS Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O9:H4 (strain HS) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|B1XBG4|CAIA_ECODH Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain K12 / DH10B) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|C4ZPW5|CAIA_ECOBW Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain K12 / MC4100 / BW2952) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|B7MNP6|CAIA_ECO81 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O81 (strain ED1a) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|B7NHE3|CAIA_ECO7I Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O7:K1 (strain IAI39 / ExPEC) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|B5YYD3|CAIA_ECO5E Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O157:H7 (strain EC4115 / EHEC) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|P60586|CAIA_ECO57 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O157:H7 GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|B7L4G2|CAIA_ECO55 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain 55989 / EAEC) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|B7MAG2|CAIA_ECO45 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O45:K1 (strain S88 / ExPEC) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|B7UI85|CAIA_ECO27 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O127:H6 (strain E2348/69 / EPEC) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|A7ZHD0|CAIA_ECO24 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O139:H28 (strain E24377A / ETEC) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|P0A9U8|YDIO_ECOLI Probable acyl-CoA dehydrogenase YdiO OS=Escherichia coli (strain K12) GN=ydiO PE=3 SV=1 134 412 8.0E-13
sp|P0A9U9|YDIO_ECOL6 Probable acyl-CoA dehydrogenase YdiO OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) GN=ydiO PE=3 SV=1 134 412 8.0E-13
sp|P0A9V0|YDIO_ECO57 Probable acyl-CoA dehydrogenase YdiO OS=Escherichia coli O157:H7 GN=ydiO PE=3 SV=1 134 412 8.0E-13
sp|B7M0D6|CAIA_ECO8A Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O8 (strain IAI1) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|Q0TLV0|CAIA_ECOL5 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O6:K15:H31 (strain 536 / UPEC) GN=caiA PE=3 SV=1 141 412 8.0E-13
sp|B3DMA2|ACD11_RAT Acyl-CoA dehydrogenase family member 11 OS=Rattus norvegicus GN=Acad11 PE=1 SV=1 75 410 2.0E-11
sp|Q80XL6|ACD11_MOUSE Acyl-CoA dehydrogenase family member 11 OS=Mus musculus GN=Acad11 PE=1 SV=2 99 410 2.0E-11
sp|Q8ZRJ7|FADE_SALTY Acyl-coenzyme A dehydrogenase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN=fadE PE=2 SV=1 32 401 5.0E-10
sp|Q8Z937|FADE_SALTI Acyl-coenzyme A dehydrogenase OS=Salmonella typhi GN=fadE PE=3 SV=1 137 401 1.0E-09
sp|Q5ZHT1|ACD11_CHICK Acyl-CoA dehydrogenase family member 11 OS=Gallus gallus GN=ACAD11 PE=2 SV=1 101 410 8.0E-09
sp|Q8X7R2|FADE_ECO57 Acyl-coenzyme A dehydrogenase OS=Escherichia coli O157:H7 GN=fadE PE=3 SV=2 137 401 1.0E-08
sp|Q47146|FADE_ECOLI Acyl-coenzyme A dehydrogenase OS=Escherichia coli (strain K12) GN=fadE PE=2 SV=2 137 401 3.0E-08
sp|Q709F0|ACD11_HUMAN Acyl-CoA dehydrogenase family member 11 OS=Homo sapiens GN=ACAD11 PE=1 SV=2 101 404 4.0E-08
sp|Q5R778|ACD11_PONAB Acyl-CoA dehydrogenase family member 11 OS=Pongo abelii GN=ACAD11 PE=2 SV=2 101 404 1.0E-07
sp|Q73ZP8|MBTN_MYCPA Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) GN=mbtN PE=3 SV=1 137 403 2.0E-07
sp|Q8ZBY6|FADE_YERPE Acyl-coenzyme A dehydrogenase OS=Yersinia pestis GN=fadE PE=3 SV=1 25 401 2.0E-06
sp|O65201|ACOX2_ARATH Acyl-coenzyme A oxidase 2, peroxisomal OS=Arabidopsis thaliana GN=ACX2 PE=1 SV=2 128 320 5.0E-06
sp|Q1BBA3|MBTN_MYCSS Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium sp. (strain MCS) GN=mbtN PE=3 SV=1 74 403 6.0E-06
sp|Q8RWZ3|IBR3_ARATH Probable acyl-CoA dehydrogenase IBR3 OS=Arabidopsis thaliana GN=IBR3 PE=1 SV=1 134 410 8.0E-06
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GO

GO Term Description Terminal node
GO:0050660 flavin adenine dinucleotide binding Yes
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors Yes
GO:0000166 nucleotide binding No
GO:0003674 molecular_function No
GO:0043167 ion binding No
GO:0005488 binding No
GO:0097159 organic cyclic compound binding No
GO:0016491 oxidoreductase activity No
GO:1901363 heterocyclic compound binding No
GO:0036094 small molecule binding No
GO:0003824 catalytic activity No
GO:0043168 anion binding No
GO:1901265 nucleoside phosphate binding No

SignalP

[Help with interpreting these statistics]
SignalP signal predicted Location
(based on Ymax)
D score
(significance: > 0.45)
No 1 - 18 0.45

Transmembrane Domains

(None)

Transcription Factor Class

(None)

Expression data

Analysis 1: Developmental stages of Agaricus bisporus (strain A15). Published in Pelkmans et al, Applied Microbiology and Biotechnology, 2016

Click here for more information

Sequences

Type of sequenceSequence
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|047910
MLSLANQTPRIIRAALASPVVNGRRAASQFAKFNWEDPLNLESQLTAEEIAIRDTAHEYCQEKLMPRVLHQWRTE
EFDHTLIPEMGQVGLLGPTIKGYGCAGVSDVAYGLIAREFERVDSGYRSTSSVQSSLVMHPIHEFGSEAQKEKYL
PRLAKGEIIGAFGLTEPDHGSDPGGMETTAEEVDGGFIVNGSKTWISNSPVADVFVIWAKCKWDNRIRGFLLEKG
AKGLTAPPIKNKIALRVSLTGSVFMDNVRVGQDSLLPGSKGLGSAFACLNSARYGISWGVMGALEDCLDRTRDYA
LQRKQFGRPIASFQLIQKKLADAQTEIALGLQASLQVGKLKGEGKLAPEMINLIKRNNCGKALQQSRALLDVFGG
NACADEYHVGRHAANLQVTNTYEGTNDIHALVLGKAITDIPAFAN*
Coding >AgabiH97|047910
ATGTTGTCTCTTGCGAACCAAACTCCACGAATAATCCGTGCGGCGCTGGCGTCGCCAGTTGTCAATGGGCGGAGG
GCAGCCAGTCAGTTTGCCAAATTCAACTGGGAAGATCCGCTGAACCTCGAATCTCAATTGACGGCGGAGGAGATT
GCCATTCGTGATACTGCCCATGAATACTGCCAGGAGAAACTTATGCCTCGAGTACTGCACCAATGGAGGACCGAA
GAATTTGACCATACTCTTATCCCAGAGATGGGCCAGGTCGGGTTATTGGGGCCTACTATCAAGGGTTATGGGTGT
GCTGGTGTGAGCGATGTCGCGTATGGTCTTATTGCACGCGAGTTTGAGCGAGTTGATTCTGGATATCGTTCAACG
TCTTCCGTACAGTCTTCACTTGTGATGCATCCCATTCATGAATTCGGTTCAGAGGCTCAGAAGGAAAAGTATCTG
CCTCGCTTGGCAAAAGGAGAGATCATTGGAGCATTTGGCTTGACCGAACCTGACCATGGATCCGATCCGGGGGGC
ATGGAGACGACCGCTGAAGAAGTCGATGGTGGTTTTATCGTCAATGGTAGCAAAACTTGGATTTCCAACTCACCT
GTCGCCGACGTGTTTGTTATCTGGGCTAAATGCAAGTGGGATAACCGCATTCGTGGCTTTCTTCTGGAAAAGGGA
GCCAAGGGTCTTACAGCACCTCCTATCAAAAACAAAATCGCTCTCCGTGTATCTCTCACCGGCTCTGTATTCATG
GACAACGTGAGAGTAGGCCAGGACTCGCTTCTTCCTGGTTCTAAAGGTCTAGGATCTGCCTTCGCATGCCTCAAC
TCTGCTCGTTACGGTATCTCCTGGGGTGTTATGGGCGCACTCGAAGATTGTCTTGACCGCACTCGCGACTATGCT
CTTCAACGCAAACAATTCGGTCGCCCCATTGCTTCTTTCCAATTGATCCAGAAAAAGCTTGCGGATGCTCAAACC
GAGATTGCGCTTGGCTTGCAAGCAAGTTTGCAAGTGGGTAAGTTGAAGGGTGAAGGAAAGCTGGCGCCGGAGATG
ATCAATTTGATCAAGAGGAATAATTGTGGTAAGGCGTTGCAGCAGAGTCGAGCTTTGTTGGATGTTTTCGGTGGC
AATGCTTGTGCCGATGAGTACCATGTTGGAAGGCATGCTGCCAACTTGCAAGTAACGAATACCTATGAGGGTACA
AATGACATTCACGCCCTTGTTCTGGGGAAAGCTATAACCGATATACCCGCATTCGCCAACTAG
Transcript >AgabiH97|047910
ATGTTGTCTCTTGCGAACCAAACTCCACGAATAATCCGTGCGGCGCTGGCGTCGCCAGTTGTCAATGGGCGGAGG
GCAGCCAGTCAGTTTGCCAAATTCAACTGGGAAGATCCGCTGAACCTCGAATCTCAATTGACGGCGGAGGAGATT
GCCATTCGTGATACTGCCCATGAATACTGCCAGGAGAAACTTATGCCTCGAGTACTGCACCAATGGAGGACCGAA
GAATTTGACCATACTCTTATCCCAGAGATGGGCCAGGTCGGGTTATTGGGGCCTACTATCAAGGGTTATGGGTGT
GCTGGTGTGAGCGATGTCGCGTATGGTCTTATTGCACGCGAGTTTGAGCGAGTTGATTCTGGATATCGTTCAACG
TCTTCCGTACAGTCTTCACTTGTGATGCATCCCATTCATGAATTCGGTTCAGAGGCTCAGAAGGAAAAGTATCTG
CCTCGCTTGGCAAAAGGAGAGATCATTGGAGCATTTGGCTTGACCGAACCTGACCATGGATCCGATCCGGGGGGC
ATGGAGACGACCGCTGAAGAAGTCGATGGTGGTTTTATCGTCAATGGTAGCAAAACTTGGATTTCCAACTCACCT
GTCGCCGACGTGTTTGTTATCTGGGCTAAATGCAAGTGGGATAACCGCATTCGTGGCTTTCTTCTGGAAAAGGGA
GCCAAGGGTCTTACAGCACCTCCTATCAAAAACAAAATCGCTCTCCGTGTATCTCTCACCGGCTCTGTATTCATG
GACAACGTGAGAGTAGGCCAGGACTCGCTTCTTCCTGGTTCTAAAGGTCTAGGATCTGCCTTCGCATGCCTCAAC
TCTGCTCGTTACGGTATCTCCTGGGGTGTTATGGGCGCACTCGAAGATTGTCTTGACCGCACTCGCGACTATGCT
CTTCAACGCAAACAATTCGGTCGCCCCATTGCTTCTTTCCAATTGATCCAGAAAAAGCTTGCGGATGCTCAAACC
GAGATTGCGCTTGGCTTGCAAGCAAGTTTGCAAGTGGGTAAGTTGAAGGGTGAAGGAAAGCTGGCGCCGGAGATG
ATCAATTTGATCAAGAGGAATAATTGTGGTAAGGCGTTGCAGCAGAGTCGAGCTTTGTTGGATGTTTTCGGTGGC
AATGCTTGTGCCGATGAGTACCATGTTGGAAGGCATGCTGCCAACTTGCAAGTAACGAATACCTATGAGGGTACA
AATGACATTCACGCCCTTGTTCTGGGGAAAGCTATAACCGATATACCCGCATTCGCCAACTAG
Gene >AgabiH97|047910
ATGTTGTCTCTTGCGAACCAAACTCCACGAATAATCCGTGCGGCGCTGGCGTCGCCAGTTGTCAATGGGCGGAGG
GCAGCCAGTCGTATGTATGACGTCGTTCGAGATTCTTTCCTTGTCTGACCTTCTACCCCAGAGTTTGCCAAATTC
AACTGGGAAGTGAGCATTGATCCTATGAGAACCTTTTCGAACACATTTCTAAGTCATTCGGTTATAGGATCCGCT
GAACCTCGAATCTCAATTGACGGCGGAGGAGATTGCCATTCGGTACGTGCATATCCTGTGCGTCCTAGAAGATGC
GTTGACCGACTTCTCTCTTAGTGATACTGCCCATGAATACTGCCAGGTATGTTCTCGCTTATAACGGCAATCAAA
TCTGCGACCTCATTCATTTGGTAGGAGAAACTTATGCCTCGAGTACTGCACCAATGGAGGACCGAAGGTGCCGTT
CCTTGTATTTCTTTCGCGTGTCGCGTTCGTTTCTGACCAGGTAATACTAATAGAATTTGACCATACTCTTATCCC
AGAGATGGGCCAGGTCGGGTTATTGGGGCCTACTATCAAGGGTTATGGGTGTGCTGGTGTGAGCGATGTCGCGTA
TGGTCTTATTGCACGCGAGTTTGAGCGGTATGTTTCTCTCCTCCTACCAGAGCATATTTACAGACATGTTGATCA
AAAACTTAGAGTTGATTCTGGATATCGTTCAACGTCTTCCGTACAGTCTTCACTTGTGATGCATCCCATTCATGA
ATTCGGTTCAGAGGCTCAGAAGGAAAAGTATCTGCCTCGCTTGGGTATGTTTCTCTTTGTCTAATCTATGACCTC
GCTTGCGAACCATAATATACAGCAAAAGGAGAGATCATTGGAGCATTTGTATGTCTATTGCACTGAACTAGCACC
GAGTATTGAATGGACCTTTAGGGCTTGACCGAACCTGACCATGGATCCGATCCGGGGGGCATGGAGACGACCGCT
GAAGAAGTCGATGGTGGTTTTATCGTCAATGGTAGCAAAACTTGGATTTCCAACTCACCTGTCGCGTTTGTCTCT
ATTCTCCCCTCCGTCGTGACATAATTATTGATTCTAATGTAGCGACGTGTTTGTTATCTGGGCTAAATGCAAGTG
GGATAACCGCATTCGTGGCTTTCTTCTGGAAAAGGTTATAAGAAAGAACTTGTCGACAATACCGTTACTCATGAA
CGCTTTGACAGGGAGCCAAGGGTCTTACAGCACCTCCTATCAAAAACAAAATCGCTCTCCGTGTATCTCTCACCG
GCTCTGTATTCATGGACAACGTGAGAGTAGGCCAGGACTCGCTTCTTCCTGGTTCTAAAGGTCTAGGATCTGCCT
TCGCATGCCTCAACTCTGCTCGGTAGGTCATTTCCCATCGCCCCAACAAGGTCAGCGTGGCTCATTTTCTCAAGT
TACGGTATCTCCTGGGGTGTTATGGGCGCACTCGAAGATTGTCTTGACCGCACTCGCGACTATGCTCTTCAACGC
AAACAATTCGGTCGCCCCATTGCTTCTTTCCAATTGATCCAGAAAAAGCTTGCGGATGCTCAAACCGAGATTGCG
CTTGGCTTGCAAGCAAGTTTGCAAGTGGGTAAGTTGAAGGGTGAAGGAAAGCTGGCGCCGGAGATGATCAATTTG
ATCAAGAGGAATAATTGTGGTAAGGCGTTGCAGCAGAGTCGAGCTTTGTTGGATGTTTTCGGTGGCAATGCTTGT
GCCGATGAGTAAGTTGATCGCCCCTCGTTGTGATATCAGAAGAAAACTAATGCTTGGACCTAATCAGGTACCATG
TTGGAAGGCATGCTGCCAACTTGCAAGTAACGAATACCTATGAGGGTACAAATGTAGGCCATTTACAGGCCATGC
CAGCAAGACAGAAATGCTGATATCTTGACTTTAGGACATTCACGCCCTTGTTCTGGGGAAAGCTATAACCGATAT
ACCCGCATTCGCCAACTAG

© 2022 - Robin Ohm - Utrecht University - The Netherlands

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