Fungal Genomics

at Utrecht University

General Properties

Protein IDHirsu2|8133
Gene name
LocationContig_511:36..1503
Strand+
Gene length (bp)1467
Transcript length (bp)1242
Coding sequence length (bp)1242
Protein length (aa) 414

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PFAM Domains

PFAM Domain ID Short name Long name E-value Start End
PF00441 Acyl-CoA_dh_1 Acyl-CoA dehydrogenase, C-terminal domain 3.8E-33 247 403
PF02770 Acyl-CoA_dh_M Acyl-CoA dehydrogenase, middle domain 1.0E-16 145 235
PF02771 Acyl-CoA_dh_N Acyl-CoA dehydrogenase, N-terminal domain 2.7E-09 15 134
PF08028 Acyl-CoA_dh_2 Acyl-CoA dehydrogenase, C-terminal domain 2.3E-06 266 369

Swissprot hits

[Show all]
Swissprot ID Swissprot Description Start End E-value
sp|Q5RBD5|IVD_PONAB Isovaleryl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=IVD PE=2 SV=1 15 395 5.0E-31
sp|P26440|IVD_HUMAN Isovaleryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=IVD PE=1 SV=1 15 395 1.0E-30
sp|P34275|IVD_CAEEL Probable acyl-CoA dehydrogenase 6 OS=Caenorhabditis elegans GN=acdh-6 PE=3 SV=2 13 399 2.0E-30
sp|Q8HXY7|ACADV_MACFA Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADVL PE=2 SV=1 111 396 5.0E-30
sp|P12007|IVD_RAT Isovaleryl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Ivd PE=1 SV=2 15 395 7.0E-29
[Show all]
[Show less]
Swissprot ID Swissprot Description Start End E-value
sp|Q5RBD5|IVD_PONAB Isovaleryl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=IVD PE=2 SV=1 15 395 5.0E-31
sp|P26440|IVD_HUMAN Isovaleryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=IVD PE=1 SV=1 15 395 1.0E-30
sp|P34275|IVD_CAEEL Probable acyl-CoA dehydrogenase 6 OS=Caenorhabditis elegans GN=acdh-6 PE=3 SV=2 13 399 2.0E-30
sp|Q8HXY7|ACADV_MACFA Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADVL PE=2 SV=1 111 396 5.0E-30
sp|P12007|IVD_RAT Isovaleryl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Ivd PE=1 SV=2 15 395 7.0E-29
sp|P49748|ACADV_HUMAN Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADVL PE=1 SV=1 114 396 8.0E-29
sp|P50544|ACADV_MOUSE Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadvl PE=1 SV=3 111 396 1.0E-28
sp|P45953|ACADV_RAT Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadvl PE=1 SV=1 111 364 2.0E-28
sp|Q3SZI8|IVD_BOVIN Isovaleryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=IVD PE=2 SV=1 15 395 4.0E-28
sp|P45867|ACDA_BACSU Acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) GN=acdA PE=2 SV=1 15 395 1.0E-27
sp|P51174|ACADL_MOUSE Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadl PE=1 SV=2 13 407 3.0E-27
sp|Q9JHI5|IVD_MOUSE Isovaleryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Ivd PE=1 SV=1 15 395 3.0E-27
sp|Q2LQP0|CHCOA_SYNAS Cyclohexane-1-carbonyl-CoA dehydrogenase OS=Syntrophus aciditrophicus (strain SB) GN=SYN_02586 PE=1 SV=1 114 395 4.0E-27
sp|Q06319|ACDS_MEGEL Acyl-CoA dehydrogenase, short-chain specific OS=Megasphaera elsdenii PE=1 SV=1 15 369 7.0E-27
sp|P15650|ACADL_RAT Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadl PE=1 SV=1 13 407 8.0E-27
sp|P45857|ACDB_BACSU Acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) GN=mmgC PE=2 SV=3 20 364 9.0E-27
sp|P48818|ACADV_BOVIN Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADVL PE=2 SV=3 111 396 2.0E-26
sp|O32176|FADE_BACSU Probable acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) GN=fadE PE=2 SV=1 5 395 2.0E-26
sp|Q60HI0|ACADL_MACFA Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADL PE=2 SV=1 13 364 3.0E-26
sp|P79274|ACADL_PIG Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Sus scrofa GN=ACADL PE=2 SV=1 13 407 3.0E-25
sp|P28330|ACADL_HUMAN Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADL PE=1 SV=2 13 364 5.0E-25
sp|Q3SZB4|ACADM_BOVIN Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADM PE=2 SV=1 3 368 1.0E-24
sp|Q9H845|ACAD9_HUMAN Acyl-CoA dehydrogenase family member 9, mitochondrial OS=Homo sapiens GN=ACAD9 PE=1 SV=1 111 408 3.0E-24
sp|C3UVB0|ACD_DESML Glutaryl-CoA dehydrogenase OS=Desulfococcus multivorans GN=Acd PE=1 SV=1 20 311 4.0E-24
sp|P11310|ACADM_HUMAN Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADM PE=1 SV=1 13 368 1.0E-23
sp|A5A6I0|ACADM_PANTR Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Pan troglodytes GN=ACADM PE=2 SV=1 13 368 2.0E-23
sp|Q9VSA3|ACADM_DROME Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Drosophila melanogaster GN=CG12262 PE=1 SV=1 15 395 6.0E-23
sp|Q8HXY8|ACADM_MACFA Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADM PE=2 SV=1 13 368 1.0E-22
sp|P16219|ACADS_HUMAN Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADS PE=1 SV=1 15 364 2.0E-22
sp|P08503|ACADM_RAT Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadm PE=1 SV=1 15 364 2.0E-22
sp|Q5RAS0|ACADS_PONAB Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=ACADS PE=2 SV=1 15 364 5.0E-22
sp|P0A9U8|YDIO_ECOLI Probable acyl-CoA dehydrogenase YdiO OS=Escherichia coli (strain K12) GN=ydiO PE=3 SV=1 71 408 8.0E-22
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 71 408 8.0E-22
sp|P0A9V0|YDIO_ECO57 Probable acyl-CoA dehydrogenase YdiO OS=Escherichia coli O157:H7 GN=ydiO PE=3 SV=1 71 408 8.0E-22
sp|P45952|ACADM_MOUSE Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadm PE=1 SV=1 15 364 1.0E-21
sp|P15651|ACADS_RAT Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acads PE=1 SV=2 15 387 2.0E-21
sp|Q8JZN5|ACAD9_MOUSE Acyl-CoA dehydrogenase family member 9, mitochondrial OS=Mus musculus GN=Acad9 PE=1 SV=2 111 408 2.0E-21
sp|Q07417|ACADS_MOUSE Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acads PE=1 SV=2 15 387 2.0E-21
sp|Q9SWG0|IVD_ARATH Isovaleryl-CoA dehydrogenase, mitochondrial OS=Arabidopsis thaliana GN=IVD PE=1 SV=2 128 364 2.0E-21
sp|A8XNF0|ACAD1_CAEBR Probable medium-chain specific acyl-CoA dehydrogenase 1, mitochondrial OS=Caenorhabditis briggsae GN=CBG15946 PE=3 SV=1 15 395 3.0E-21
sp|Q9FS87|IVD_SOLTU Isovaleryl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum GN=IVD PE=1 SV=2 6 364 5.0E-21
sp|O34421|ACDC_BACSU Probable acyl-CoA dehydrogenase YngJ OS=Bacillus subtilis (strain 168) GN=yngJ PE=3 SV=1 17 364 5.0E-21
sp|P81140|GCDH_PIG Glutaryl-CoA dehydrogenase, mitochondrial (Fragment) OS=Sus scrofa GN=GCDH PE=1 SV=1 25 368 7.0E-21
sp|Q75IM9|IVD_ORYSJ Isovaleryl-CoA dehydrogenase, mitochondrial OS=Oryza sativa subsp. japonica GN=Os05g0125500 PE=2 SV=2 13 364 1.0E-20
sp|Q22347|ACADM_CAEEL Probable medium-chain specific acyl-CoA dehydrogenase 10, mitochondrial OS=Caenorhabditis elegans GN=acdh-10 PE=2 SV=1 15 395 3.0E-20
sp|Q9FS88|MBCD_SOLTU 2-methylacyl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum GN=2MBCD PE=1 SV=2 6 364 3.0E-20
sp|Q0T8F5|CAIA_SHIF8 Crotonobetainyl-CoA dehydrogenase OS=Shigella flexneri serotype 5b (strain 8401) GN=caiA PE=3 SV=1 139 395 5.0E-20
sp|Q2KHZ9|GCDH_BOVIN Glutaryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=GCDH PE=2 SV=1 48 368 5.0E-20
sp|B7M0D6|CAIA_ECO8A Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O8 (strain IAI1) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|Q20772|GCDH_CAEEL Probable glutaryl-CoA dehydrogenase, mitochondrial OS=Caenorhabditis elegans GN=F54D5.7 PE=1 SV=1 5 367 7.0E-20
sp|Q3Z5W9|CAIA_SHISS Crotonobetainyl-CoA dehydrogenase OS=Shigella sonnei (strain Ss046) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|P60587|CAIA_SHIFL Crotonobetainyl-CoA dehydrogenase OS=Shigella flexneri GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|Q32K58|CAIA_SHIDS Crotonobetainyl-CoA dehydrogenase OS=Shigella dysenteriae serotype 1 (strain Sd197) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|B7LWN0|CAIA_ESCF3 Crotonobetainyl-CoA dehydrogenase OS=Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|Q1RGF9|CAIA_ECOUT Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain UTI89 / UPEC) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|B1LFX2|CAIA_ECOSM Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain SMS-3-5 / SECEC) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|B6HYZ0|CAIA_ECOSE Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain SE11) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|B7N7R4|CAIA_ECOLU Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|P60584|CAIA_ECOLI Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain K12) GN=caiA PE=1 SV=1 139 395 7.0E-20
sp|B1IRD7|CAIA_ECOLC Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|P60585|CAIA_ECOL6 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|A1A789|CAIA_ECOK1 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O1:K1 / APEC GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|A7ZVY9|CAIA_ECOHS Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O9:H4 (strain HS) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|B1XBG4|CAIA_ECODH Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain K12 / DH10B) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|C4ZPW5|CAIA_ECOBW Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain K12 / MC4100 / BW2952) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|B7MNP6|CAIA_ECO81 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O81 (strain ED1a) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|B7NHE3|CAIA_ECO7I Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O7:K1 (strain IAI39 / ExPEC) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|B5YYD3|CAIA_ECO5E Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O157:H7 (strain EC4115 / EHEC) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|P60586|CAIA_ECO57 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O157:H7 GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|B7L4G2|CAIA_ECO55 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain 55989 / EAEC) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|B7MAG2|CAIA_ECO45 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O45:K1 (strain S88 / ExPEC) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|B7UI85|CAIA_ECO27 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O127:H6 (strain E2348/69 / EPEC) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|A7ZHD0|CAIA_ECO24 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O139:H28 (strain E24377A / ETEC) GN=caiA PE=3 SV=1 139 395 7.0E-20
sp|Q0TLV0|CAIA_ECOL5 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O6:K15:H31 (strain 536 / UPEC) GN=caiA PE=3 SV=1 139 395 8.0E-20
sp|Q8Z9L2|CAIA_SALTI Crotonobetainyl-CoA dehydrogenase OS=Salmonella typhi GN=caiA PE=3 SV=1 139 395 1.0E-19
sp|Q8ZRX2|CAIA_SALTY Crotonobetainyl-CoA dehydrogenase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|B4TWR6|CAIA_SALSV Crotonobetainyl-CoA dehydrogenase OS=Salmonella schwarzengrund (strain CVM19633) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|B5BL57|CAIA_SALPK Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi A (strain AKU_12601) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|C0Q4L5|CAIA_SALPC Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi C (strain RKS4594) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|A9MYJ9|CAIA_SALPB Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|Q5PIN6|CAIA_SALPA Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi A (strain ATCC 9150 / SARB42) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|B4T6J8|CAIA_SALNS Crotonobetainyl-CoA dehydrogenase OS=Salmonella newport (strain SL254) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|B4TIH2|CAIA_SALHS Crotonobetainyl-CoA dehydrogenase OS=Salmonella heidelberg (strain SL476) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|B5RGA6|CAIA_SALG2 Crotonobetainyl-CoA dehydrogenase OS=Salmonella gallinarum (strain 287/91 / NCTC 13346) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|B5R1R2|CAIA_SALEP Crotonobetainyl-CoA dehydrogenase OS=Salmonella enteritidis PT4 (strain P125109) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|B5FHG7|CAIA_SALDC Crotonobetainyl-CoA dehydrogenase OS=Salmonella dublin (strain CT_02021853) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|Q57TI8|CAIA_SALCH Crotonobetainyl-CoA dehydrogenase OS=Salmonella choleraesuis (strain SC-B67) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|B5F752|CAIA_SALA4 Crotonobetainyl-CoA dehydrogenase OS=Salmonella agona (strain SL483) GN=caiA PE=3 SV=1 139 395 2.0E-19
sp|P41367|ACADM_PIG Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Sus scrofa GN=ACADM PE=1 SV=3 15 368 2.0E-19
sp|A9MQH5|CAIA_SALAR Crotonobetainyl-CoA dehydrogenase OS=Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980) GN=caiA PE=3 SV=1 139 395 7.0E-19
sp|Q8GB20|CAIA_PROSL Crotonobetainyl-CoA dehydrogenase OS=Proteus sp. (strain LE138) GN=caiA PE=3 SV=1 116 395 8.0E-19
sp|B4EY23|CAIA_PROMH Crotonobetainyl-CoA dehydrogenase OS=Proteus mirabilis (strain HI4320) GN=caiA PE=3 SV=1 116 395 8.0E-19
sp|A8ALR4|CAIA_CITK8 Crotonobetainyl-CoA dehydrogenase OS=Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) GN=caiA PE=3 SV=1 139 395 1.0E-18
sp|P79273|ACADS_PIG Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Sus scrofa GN=ACADS PE=2 SV=1 15 364 2.0E-18
sp|G3KIM8|ACRC_CLOPR Acryloyl-CoA reductase (NADH) OS=Clostridium propionicum GN=acrC PE=1 SV=1 115 406 3.0E-18
sp|A8WP91|ACAD2_CAEBR Probable medium-chain specific acyl-CoA dehydrogenase 2, mitochondrial OS=Caenorhabditis briggsae GN=CBG00953 PE=3 SV=2 15 306 7.0E-18
sp|Q54R47|GCDH_DICDI Glutaryl-CoA dehydrogenase, mitochondrial OS=Dictyostelium discoideum GN=gcdh PE=3 SV=1 108 367 8.0E-18
sp|Q60759|GCDH_MOUSE Glutaryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Gcdh PE=1 SV=2 48 368 1.0E-17
sp|Q8HXX8|GCDH_MACFA Glutaryl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=GCDH PE=2 SV=1 48 368 1.0E-17
sp|Q3ZBF6|ACADS_BOVIN Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADS PE=1 SV=1 15 364 2.0E-17
sp|P9WQG1|ACDP_MYCTU Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=fadE25 PE=1 SV=1 5 395 5.0E-17
sp|P9WQG0|ACDP_MYCTO Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=fadE25 PE=3 SV=1 5 395 5.0E-17
sp|P63428|ACDP_MYCBO Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=fadE25 PE=3 SV=1 5 395 5.0E-17
sp|Q92947|GCDH_HUMAN Glutaryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=GCDH PE=1 SV=1 48 368 6.0E-17
sp|Q2LQN9|CH1CO_SYNAS Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase OS=Syntrophus aciditrophicus (strain SB) GN=SYN_02587 PE=1 SV=1 146 395 6.0E-17
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 20 395 8.0E-17
sp|Q54IM8|ACAD8_DICDI Isobutyryl-CoA dehydrogenase, mitochondrial OS=Dictyostelium discoideum GN=acad8 PE=3 SV=1 15 396 4.0E-16
sp|Q9D7B6|ACAD8_MOUSE Isobutyryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acad8 PE=1 SV=2 147 407 1.0E-15
sp|Q0NXR6|ACAD8_BOVIN Isobutyryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACAD8 PE=2 SV=1 147 396 2.0E-15
sp|P63430|Y897_MYCBO Probable acyl-CoA dehydrogenase FadE10 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=fadE10 PE=3 SV=1 111 405 2.0E-15
sp|P9WQF7|Y873_MYCTU Probable acyl-CoA dehydrogenase FadE10 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=fadE10 PE=1 SV=1 111 405 2.0E-15
sp|P9WQF6|Y873_MYCTO Probable acyl-CoA dehydrogenase FadE10 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=fadE10 PE=3 SV=1 111 405 2.0E-15
sp|Q9UKU7|ACAD8_HUMAN Isobutyryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACAD8 PE=1 SV=1 147 406 3.0E-15
sp|P46703|ACDP_MYCLE Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium leprae (strain TN) GN=fadE25 PE=3 SV=1 5 395 3.0E-13
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 96 399 7.0E-13
sp|Q9DBL1|ACDSB_MOUSE Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadsb PE=1 SV=1 15 395 6.0E-12
sp|Q5RF40|ACDSB_PONAB Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=ACADSB PE=2 SV=1 138 395 2.0E-11
sp|P45954|ACDSB_HUMAN Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADSB PE=1 SV=1 138 395 2.0E-11
sp|Q5EAD4|ACDSB_BOVIN Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADSB PE=2 SV=1 138 395 5.0E-11
sp|Q1BBA3|MBTN_MYCSS Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium sp. (strain MCS) GN=mbtN PE=3 SV=1 29 406 8.0E-11
sp|P70584|ACDSB_RAT Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadsb PE=1 SV=1 146 312 9.0E-11
sp|Q5LLW7|DMDC_RUEPO 3-methylmercaptopropionyl-CoA dehydrogenase OS=Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) GN=dmdC PE=1 SV=1 121 407 1.0E-10
sp|Q54RR5|ACDSB_DICDI Probable short/branched chain specific acyl-CoA dehydrogenase OS=Dictyostelium discoideum GN=acadsb PE=3 SV=1 145 410 9.0E-10
sp|P9WQF9|MBTN_MYCTU Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=mbtN PE=1 SV=1 111 399 4.0E-09
sp|P9WQF8|MBTN_MYCTO Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=mbtN PE=3 SV=1 111 399 4.0E-09
sp|P63432|MBTN_MYCBO Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=mbtN PE=3 SV=1 111 399 4.0E-09
sp|P33224|AIDB_ECOLI Putative acyl-CoA dehydrogenase AidB OS=Escherichia coli (strain K12) GN=aidB PE=1 SV=3 144 317 2.0E-08
sp|Q5R778|ACD11_PONAB Acyl-CoA dehydrogenase family member 11 OS=Pongo abelii GN=ACAD11 PE=2 SV=2 120 369 1.0E-07
sp|P9WQG3|ACDC_MYCTU Acyl-CoA dehydrogenase fadE12 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=fadE12 PE=1 SV=1 114 369 1.0E-07
sp|P9WQG2|ACDC_MYCTO Acyl-CoA dehydrogenase fadE12 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=fadE12 PE=3 SV=1 114 369 1.0E-07
sp|Q6JQN1|ACD10_HUMAN Acyl-CoA dehydrogenase family member 10 OS=Homo sapiens GN=ACAD10 PE=1 SV=1 137 368 1.0E-07
sp|Q7U0Y2|ACDC_MYCBO Acyl-CoA dehydrogenase fadE12 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=fadE12 PE=3 SV=1 114 369 2.0E-07
sp|Q8K370|ACD10_MOUSE Acyl-CoA dehydrogenase family member 10 OS=Mus musculus GN=Acad10 PE=1 SV=1 137 368 2.0E-07
sp|Q709F0|ACD11_HUMAN Acyl-CoA dehydrogenase family member 11 OS=Homo sapiens GN=ACAD11 PE=1 SV=2 120 369 3.0E-07
sp|Q8RWZ3|IBR3_ARATH Probable acyl-CoA dehydrogenase IBR3 OS=Arabidopsis thaliana GN=IBR3 PE=1 SV=1 137 395 3.0E-07
sp|Q96329|ACOX4_ARATH Acyl-coenzyme A oxidase 4, peroxisomal OS=Arabidopsis thaliana GN=ACX4 PE=1 SV=1 145 367 5.0E-07
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GO

GO Term Description Terminal node
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors Yes
GO:0055114 oxidation-reduction process Yes
GO:0050660 flavin adenine dinucleotide binding Yes
GO:0008152 metabolic process No
GO:1901265 nucleoside phosphate binding No
GO:1901363 heterocyclic compound binding No
GO:0008150 biological_process No
GO:0048037 cofactor binding No
GO:0036094 small molecule binding No
GO:0000166 nucleotide binding No
GO:0043167 ion binding No
GO:0016491 oxidoreductase activity No
GO:0097159 organic cyclic compound binding No
GO:0003674 molecular_function No
GO:0043168 anion binding No
GO:0003824 catalytic activity No
GO:0005488 binding No
GO:0050662 coenzyme binding No

SignalP

[Help with interpreting these statistics]
SignalP signal predicted Location
(based on Ymax)
D score
(significance: > 0.45)
No 1 - 23 0.45

Transmembrane Domains

(None)

Transcription Factor Class

(None)

Expression data

No expression data available for this genome

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 >Hirsu2|8133
LAPGDAFRSPPYYGDSHRRLQRAARDFVDRHLRPEAQESEPAGRYISQDLVDRMSRLGILHMRMGPGPHLHGVEL
LGGAVDGRDFDYFHELALNQEMARITARGFQDGTMAGMAIGLSAVLNFARDEAWKRAVADRVLSGRKKICLAVTE
AFAGSDVAGLRTTADKTPDGKHYIVNGTKKWITNGMWCDYFVTAVRTGNALSVLLIERGDGVETKAIKTSYSAAA
GTAFVTFDDVKVPAENLLGEENKGMRVILSNFNHERWMMVGATLANCRLVVEESLKWANQRIVFGKPLIEQPVIR
QKLAKMIALVEANQSWLESITYQMCHMPYHQQAKHLAGPIGLLKMSSTRAAHEIADEAVQIWGGRALTQTGMGKH
IEMFNRTYKFDAILGGAEEVLADLGVRQAMRNFPKAML*
Coding >Hirsu2|8133
CTGGCGCCCGGCGACGCCTTCCGGAGCCCGCCCTACTACGGCGACTCGCACCGCCGCCTGCAGCGCGCCGCCCGC
GACTTCGTCGACCGCCACCTGCGGCCCGAGGCCCAAGAGTCCGAGCCGGCCGGCCGCTACATCAGCCAGGACCTC
GTCGACCGCATGAGCCGGCTCGGCATCCTGCACATGCGCATGGGGCCCGGCCCACACCTGCACGGCGTCGAGCTG
CTGGGCGGCGCCGTCGACGGCCGTGACTTCGACTACTTCCACGAGCTCGCCCTCAACCAGGAGATGGCCCGCATC
ACGGCCCGCGGCTTCCAGGACGGCACCATGGCCGGCATGGCCATCGGCCTCTCCGCCGTCCTCAACTTCGCCCGC
GACGAGGCCTGGAAGCGCGCCGTCGCCGACCGCGTCCTGTCCGGCCGCAAGAAGATCTGCCTCGCCGTCACCGAG
GCCTTCGCCGGCTCCGACGTTGCCGGCCTGCGCACCACGGCCGACAAGACGCCCGACGGCAAACACTACATCGTC
AACGGCACCAAGAAGTGGATCACCAACGGCATGTGGTGCGACTACTTCGTCACCGCCGTCCGCACCGGCAACGCC
CTCAGCGTCCTGCTGATCGAGAGGGGCGACGGCGTCGAGACCAAGGCCATCAAGACGTCCTACTCCGCCGCCGCC
GGCACCGCCTTCGTCACCTTCGACGACGTCAAGGTGCCGGCCGAGAACCTGCTGGGCGAGGAGAACAAGGGCATG
CGCGTCATCCTGAGCAACTTCAACCACGAACGCTGGATGATGGTTGGAGCCACTCTCGCCAACTGCAGGCTTGTC
GTCGAGGAGTCCCTCAAGTGGGCGAACCAGCGTATCGTCTTCGGCAAGCCTCTCATCGAACAACCCGTCATCCGG
CAAAAACTCGCCAAGATGATTGCCCTCGTCGAAGCCAACCAGTCGTGGCTCGAGTCCATCACCTACCAGATGTGC
CATATGCCCTACCACCAGCAGGCCAAGCACCTCGCCGGCCCCATCGGCCTCCTCAAGATGAGCTCCACGCGCGCC
GCCCACGAGATTGCCGACGAGGCCGTGCAGATCTGGGGCGGCCGTGCTCTGACCCAGACGGGCATGGGCAAGCAC
ATCGAGATGTTCAACCGAACCTACAAGTTCGATGCCATCCTTGGTGGTGCCGAGGAGGTGCTGGCCGACCTCGGT
GTGCGCCAGGCTATGCGGAACTTCCCCAAAGCCATGCTGTGA
Transcript >Hirsu2|8133
CTGGCGCCCGGCGACGCCTTCCGGAGCCCGCCCTACTACGGCGACTCGCACCGCCGCCTGCAGCGCGCCGCCCGC
GACTTCGTCGACCGCCACCTGCGGCCCGAGGCCCAAGAGTCCGAGCCGGCCGGCCGCTACATCAGCCAGGACCTC
GTCGACCGCATGAGCCGGCTCGGCATCCTGCACATGCGCATGGGGCCCGGCCCACACCTGCACGGCGTCGAGCTG
CTGGGCGGCGCCGTCGACGGCCGTGACTTCGACTACTTCCACGAGCTCGCCCTCAACCAGGAGATGGCCCGCATC
ACGGCCCGCGGCTTCCAGGACGGCACCATGGCCGGCATGGCCATCGGCCTCTCCGCCGTCCTCAACTTCGCCCGC
GACGAGGCCTGGAAGCGCGCCGTCGCCGACCGCGTCCTGTCCGGCCGCAAGAAGATCTGCCTCGCCGTCACCGAG
GCCTTCGCCGGCTCCGACGTTGCCGGCCTGCGCACCACGGCCGACAAGACGCCCGACGGCAAACACTACATCGTC
AACGGCACCAAGAAGTGGATCACCAACGGCATGTGGTGCGACTACTTCGTCACCGCCGTCCGCACCGGCAACGCC
CTCAGCGTCCTGCTGATCGAGAGGGGCGACGGCGTCGAGACCAAGGCCATCAAGACGTCCTACTCCGCCGCCGCC
GGCACCGCCTTCGTCACCTTCGACGACGTCAAGGTGCCGGCCGAGAACCTGCTGGGCGAGGAGAACAAGGGCATG
CGCGTCATCCTGAGCAACTTCAACCACGAACGCTGGATGATGGTTGGAGCCACTCTCGCCAACTGCAGGCTTGTC
GTCGAGGAGTCCCTCAAGTGGGCGAACCAGCGTATCGTCTTCGGCAAGCCTCTCATCGAACAACCCGTCATCCGG
CAAAAACTCGCCAAGATGATTGCCCTCGTCGAAGCCAACCAGTCGTGGCTCGAGTCCATCACCTACCAGATGTGC
CATATGCCCTACCACCAGCAGGCCAAGCACCTCGCCGGCCCCATCGGCCTCCTCAAGATGAGCTCCACGCGCGCC
GCCCACGAGATTGCCGACGAGGCCGTGCAGATCTGGGGCGGCCGTGCTCTGACCCAGACGGGCATGGGCAAGCAC
ATCGAGATGTTCAACCGAACCTACAAGTTCGATGCCATCCTTGGTGGTGCCGAGGAGGTGCTGGCCGACCTCGGT
GTGCGCCAGGCTATGCGGAACTTCCCCAAAGCCATGCTGTGA
Gene >Hirsu2|8133
CTGGCGCCCGGCGACGCCTTCCGGAGCCCGCCCTACTACGGCGACTCGCACCGCCGCCTGCAGCGCGCCGCCCGC
GACTTCGTCGACCGCCACCTGCGGCCCGAGGCCCAAGAGTCCGAGCCGGCCGGCCGCTACATCAGCCAGGACCTC
GTCGACCGCATGAGCCGGCTCGGCATCCTGCACATGCGCATGGGGCCCGGCCCACACCTGCACGGCGTCGAGCTG
CTGGGCGGCGCCGTCGACGGCCGTGACTTCGACTACTTCCACGAGCTCGCCCTCAACCAGGAGATGGCCCGCATC
ACGGCCCGCGGCTTCCAGGACGGCACCATGGCCGGCATGGCCATCGGCCTCTCCGCCGTCCTCAACTTCGCCCGC
GACGAGGCCTGGAAGCGCGCCGTCGCCGACCGCGTCCTGTCCGGCCGCAAGAAGATCTGCCTCGCCGTCACCGAG
GCCTTCGCCGGCTCCGACGTTGCCGGCCTGCGCACCACGGCCGACAAGACGCCCGACGGCAAACACTACGTGAGC
AGTCGATCCAACGCGTCGGCGGGAACAAGTCGTGCTGACACGAGCCCTCCCAGATCGTCAACGGCACCAAGAAGT
GGATCACCAACGGCATGTGGTGCGACTACTTCGTCACCGCCGTCCGCACCGGCAACGCCCTCAGCGTCCTGCTGA
TCGAGAGGGGCGACGGCGTCGAGACCAAGGCCATCAAGACGTCCTACTCCGCCGCCGCCGGCACCGCCTTCGTCA
CCTTCGACGACGTCAAGGTGCCGGCCGAGAACCTGCTGGGCGAGGAGAACAAGGGCATGCGCGTCATCCTGAGCA
ACTTCAACCACGAACGCTGGATGATGGTTGGTGCGTCCACGTCGCCCGTCAAGCTCCCAGCAGCACCCGGTCAAC
GCGATGCTGATGCCAGAAACCCAATAGGAGCCACTCTCGCCAACTGCAGGCTTGTCGTCGAGGAGTCCCTCAAGT
GGGCGAACCAGCGTATCGTCTTCGGCAAGCCTCTCATCGAACAACCCGTCATCCGGCAAAAGTAAGAAACCTCTT
GCTGTCCTCTCTTTTCACTGGGCCCCCGTCGCCCGTTGGATGCTGTCGAGCGCAGGAACTTACCAGCCCTCTCGT
CGCAGACTCGCCAAGATGATTGCCCTCGTCGAAGCCAACCAGTCGTGGCTCGAGTCCATCACCTACCAGATGTGC
CATATGCCCTACCACCAGCAGGCCAAGCACCTCGCCGGCCCCATCGGCCTCCTCAAGATGAGCTCCACGCGCGCC
GCCCACGAGATTGCCGACGAGGCCGTGCAGATCTGGGGCGGCCGTGCTCTGACCCAGACGGGCATGGGCAAGCAC
ATCGAGATGTTCAACCGAACCTACAAGTTCGATGCCATCCTTGGTGGTGCCGAGGAGGTGCTGGCCGACCTCGGT
GTGCGCCAGGCTATGCGGAACTTCCCCAAAGCCATGCTGTGA

© 2022 - Robin Ohm - Utrecht University - The Netherlands

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