Fungal Genomics

at Utrecht University

General Properties

Protein IDAgabiH97|085860
Gene name
Locationscaffold_5:1906818..1908026
Strand+
Gene length (bp)1208
Transcript length (bp)891
Coding sequence length (bp)891
Protein length (aa) 297

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PFAM Domains

PFAM Domain ID Short name Long name E-value Start End
PF00378 ECH_1 Enoyl-CoA hydratase/isomerase 5.8E-36 16 270
PF16113 ECH_2 Enoyl-CoA hydratase/isomerase 1.6E-14 19 260

Swissprot hits

[Show all]
Swissprot ID Swissprot Description Start End E-value
sp|A4YI89|HPCD_METS5 3-hydroxypropionyl-coenzyme A dehydratase OS=Metallosphaera sedula (strain ATCC 51363 / DSM 5348) GN=Msed_2001 PE=1 SV=1 5 271 4.0E-25
sp|Q1ZXF1|ECHM_DICDI Probable enoyl-CoA hydratase, mitochondrial OS=Dictyostelium discoideum GN=echs1 PE=3 SV=1 3 269 5.0E-24
sp|P9WNP1|ECHA6_MYCTU Probable enoyl-CoA hydratase echA6 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=echA6 PE=1 SV=1 9 271 2.0E-20
sp|P9WNP0|ECHA6_MYCTO Probable enoyl-CoA hydratase echA6 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=echA6 PE=3 SV=1 9 271 2.0E-20
sp|P64015|ECHA6_MYCBO Probable enoyl-CoA hydratase echA6 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=echA6 PE=3 SV=1 9 271 2.0E-20
[Show all]
[Show less]
Swissprot ID Swissprot Description Start End E-value
sp|A4YI89|HPCD_METS5 3-hydroxypropionyl-coenzyme A dehydratase OS=Metallosphaera sedula (strain ATCC 51363 / DSM 5348) GN=Msed_2001 PE=1 SV=1 5 271 4.0E-25
sp|Q1ZXF1|ECHM_DICDI Probable enoyl-CoA hydratase, mitochondrial OS=Dictyostelium discoideum GN=echs1 PE=3 SV=1 3 269 5.0E-24
sp|P9WNP1|ECHA6_MYCTU Probable enoyl-CoA hydratase echA6 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=echA6 PE=1 SV=1 9 271 2.0E-20
sp|P9WNP0|ECHA6_MYCTO Probable enoyl-CoA hydratase echA6 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=echA6 PE=3 SV=1 9 271 2.0E-20
sp|P64015|ECHA6_MYCBO Probable enoyl-CoA hydratase echA6 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=echA6 PE=3 SV=1 9 271 2.0E-20
sp|A8ALR7|CAID_CITK8 Carnitinyl-CoA dehydratase OS=Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) GN=caiD PE=3 SV=1 13 271 5.0E-20
sp|P9WNN9|ECHA8_MYCTU Probable enoyl-CoA hydratase echA8 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=echA8 PE=1 SV=1 6 270 7.0E-20
sp|P9WNN8|ECHA8_MYCTO Probable enoyl-CoA hydratase echA8 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=echA8 PE=3 SV=1 6 270 7.0E-20
sp|P64017|ECHA8_MYCBO Probable enoyl-CoA hydratase echA8 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=echA8 PE=3 SV=1 6 270 7.0E-20
sp|P76082|PAAF_ECOLI 2,3-dehydroadipyl-CoA hydratase OS=Escherichia coli (strain K12) GN=paaF PE=1 SV=1 6 271 9.0E-20
sp|Q86YB7|ECHD2_HUMAN Enoyl-CoA hydratase domain-containing protein 2, mitochondrial OS=Homo sapiens GN=ECHDC2 PE=1 SV=2 14 271 1.0E-19
sp|Q8BH95|ECHM_MOUSE Enoyl-CoA hydratase, mitochondrial OS=Mus musculus GN=Echs1 PE=1 SV=1 13 269 2.0E-19
sp|Q8GB17|CAID_PROSL Carnitinyl-CoA dehydratase OS=Proteus sp. (strain LE138) GN=caiD PE=1 SV=3 15 271 7.0E-19
sp|B4EY26|CAID_PROMH Carnitinyl-CoA dehydratase OS=Proteus mirabilis (strain HI4320) GN=caiD PE=3 SV=1 15 271 7.0E-19
sp|Q8Z9L5|CAID_SALTI Carnitinyl-CoA dehydratase OS=Salmonella typhi GN=caiD PE=3 SV=3 7 271 7.0E-19
sp|B4T6J5|CAID_SALNS Carnitinyl-CoA dehydratase OS=Salmonella newport (strain SL254) GN=caiD PE=3 SV=1 7 271 7.0E-19
sp|B5RGA4|CAID_SALG2 Carnitinyl-CoA dehydratase OS=Salmonella gallinarum (strain 287/91 / NCTC 13346) GN=caiD PE=3 SV=1 7 271 8.0E-19
sp|B5R1Q9|CAID_SALEP Carnitinyl-CoA dehydratase OS=Salmonella enteritidis PT4 (strain P125109) GN=caiD PE=3 SV=1 7 271 8.0E-19
sp|Q8ZRX5|CAID_SALTY Carnitinyl-CoA dehydratase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN=caiD PE=3 SV=3 7 271 1.0E-18
sp|B4TWR3|CAID_SALSV Carnitinyl-CoA dehydratase OS=Salmonella schwarzengrund (strain CVM19633) GN=caiD PE=3 SV=1 7 271 1.0E-18
sp|B4TIG9|CAID_SALHS Carnitinyl-CoA dehydratase OS=Salmonella heidelberg (strain SL476) GN=caiD PE=3 SV=1 7 271 1.0E-18
sp|B5BL54|CAID_SALPK Carnitinyl-CoA dehydratase OS=Salmonella paratyphi A (strain AKU_12601) GN=caiD PE=3 SV=1 7 271 1.0E-18
sp|C0Q4L2|CAID_SALPC Carnitinyl-CoA dehydratase OS=Salmonella paratyphi C (strain RKS4594) GN=caiD PE=3 SV=1 7 271 1.0E-18
sp|Q5PIL1|CAID_SALPA Carnitinyl-CoA dehydratase OS=Salmonella paratyphi A (strain ATCC 9150 / SARB42) GN=caiD PE=3 SV=1 7 271 1.0E-18
sp|Q57TJ1|CAID_SALCH Carnitinyl-CoA dehydratase OS=Salmonella choleraesuis (strain SC-B67) GN=caiD PE=3 SV=1 7 271 1.0E-18
sp|B5F749|CAID_SALA4 Carnitinyl-CoA dehydratase OS=Salmonella agona (strain SL483) GN=caiD PE=3 SV=1 7 271 1.0E-18
sp|A9MYJ5|CAID_SALPB Carnitinyl-CoA dehydratase OS=Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) GN=caiD PE=3 SV=1 7 271 1.0E-18
sp|B5FHG4|CAID_SALDC Carnitinyl-CoA dehydratase OS=Salmonella dublin (strain CT_02021853) GN=caiD PE=3 SV=1 7 271 1.0E-18
sp|P14604|ECHM_RAT Enoyl-CoA hydratase, mitochondrial OS=Rattus norvegicus GN=Echs1 PE=1 SV=1 13 269 2.0E-18
sp|A9MR28|CAID_SALAR Carnitinyl-CoA dehydratase OS=Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980) GN=caiD PE=3 SV=1 7 271 3.0E-18
sp|Q8XA35|CAID_ECO57 Carnitinyl-CoA dehydratase OS=Escherichia coli O157:H7 GN=caiD PE=3 SV=3 7 271 5.0E-18
sp|Q58DM8|ECHM_BOVIN Enoyl-CoA hydratase, mitochondrial OS=Bos taurus GN=ECHS1 PE=2 SV=1 13 269 6.0E-18
sp|O34893|YNGF_BACSU Putative enoyl-CoA hydratase/isomerase YngF OS=Bacillus subtilis (strain 168) GN=yngF PE=3 SV=1 20 272 8.0E-18
sp|P59395|CAID_SHIFL Carnitinyl-CoA dehydratase OS=Shigella flexneri GN=caiD PE=3 SV=2 7 271 9.0E-18
sp|P31551|CAID_ECOLI Carnitinyl-CoA dehydratase OS=Escherichia coli (strain K12) GN=caiD PE=1 SV=4 7 271 1.0E-17
sp|B1IRE0|CAID_ECOLC Carnitinyl-CoA dehydratase OS=Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) GN=caiD PE=3 SV=1 7 271 1.0E-17
sp|Q8FLA6|CAID_ECOL6 Carnitinyl-CoA dehydratase OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) GN=caiD PE=3 SV=3 7 271 1.0E-17
sp|Q0TLV3|CAID_ECOL5 Carnitinyl-CoA dehydratase OS=Escherichia coli O6:K15:H31 (strain 536 / UPEC) GN=caiD PE=3 SV=1 7 271 1.0E-17
sp|B1LFW9|CAID_ECOSM Carnitinyl-CoA dehydratase OS=Escherichia coli (strain SMS-3-5 / SECEC) GN=caiD PE=3 SV=1 7 271 1.0E-17
sp|Q50130|ECHA6_MYCLE Probable enoyl-CoA hydratase echA6 OS=Mycobacterium leprae (strain TN) GN=echA6 PE=3 SV=1 9 271 2.0E-17
sp|P52046|CRT_CLOAB Short-chain-enoyl-CoA hydratase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) GN=crt PE=1 SV=1 5 265 3.0E-17
sp|P30084|ECHM_HUMAN Enoyl-CoA hydratase, mitochondrial OS=Homo sapiens GN=ECHS1 PE=1 SV=4 13 269 3.0E-17
sp|Q5R646|ECHM_PONAB Enoyl-CoA hydratase, mitochondrial OS=Pongo abelii GN=ECHS1 PE=2 SV=1 13 269 6.0E-17
sp|P77467|PAAG_ECOLI 1,2-epoxyphenylacetyl-CoA isomerase OS=Escherichia coli (strain K12) GN=paaG PE=1 SV=1 17 271 6.0E-17
sp|P41942|YKB4_CAEEL Uncharacterized protein B0272.4 OS=Caenorhabditis elegans GN=B0272.4 PE=3 SV=1 9 195 8.0E-17
sp|O07137|ECHA8_MYCLE Probable enoyl-CoA hydratase echA8 OS=Mycobacterium leprae (strain TN) GN=echA8 PE=3 SV=1 6 270 1.0E-16
sp|Q3TLP5|ECHD2_MOUSE Enoyl-CoA hydratase domain-containing protein 2, mitochondrial OS=Mus musculus GN=Echdc2 PE=1 SV=2 17 271 7.0E-16
sp|Q2TBT3|ECHD2_BOVIN Enoyl-CoA hydratase domain-containing protein 2, mitochondrial OS=Bos taurus GN=ECHDC2 PE=2 SV=1 17 271 5.0E-15
sp|P34559|ECHM_CAEEL Probable enoyl-CoA hydratase, mitochondrial OS=Caenorhabditis elegans GN=ech-6 PE=3 SV=1 9 269 7.0E-14
sp|Q54SS0|ECH1_DICDI Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial OS=Dictyostelium discoideum GN=ech1 PE=3 SV=1 18 269 8.0E-13
sp|Q9LCU3|CBAD2_ARTSP 4-chlorobenzoyl coenzyme A dehalogenase-2 OS=Arthrobacter sp. GN=fcbB2 PE=1 SV=1 1 264 5.0E-12
sp|O85078|CBAD1_ARTSP 4-chlorobenzoyl coenzyme A dehalogenase-1 OS=Arthrobacter sp. GN=fcbB1 PE=1 SV=2 1 264 7.0E-12
sp|Q869N6|CRTL_DICDI 3-hydroxybutyryl-CoA dehydratase-like protein, mitochondrial OS=Dictyostelium discoideum GN=DDB_G0271866 PE=3 SV=1 20 276 2.0E-11
sp|Q52995|ECHH_RHIME Probable enoyl-CoA hydratase OS=Rhizobium meliloti (strain 1021) GN=fadB1 PE=3 SV=2 6 269 3.0E-11
sp|P94549|FADB_BACSU Probable enoyl-CoA hydratase OS=Bacillus subtilis (strain 168) GN=fadB PE=2 SV=1 9 271 5.0E-11
sp|Q9WUR2|ECI2_MOUSE Enoyl-CoA delta isomerase 2, mitochondrial OS=Mus musculus GN=Eci2 PE=1 SV=2 7 195 9.0E-11
sp|O35459|ECH1_MOUSE Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial OS=Mus musculus GN=Ech1 PE=1 SV=1 2 268 2.0E-10
sp|O75521|ECI2_HUMAN Enoyl-CoA delta isomerase 2, mitochondrial OS=Homo sapiens GN=ECI2 PE=1 SV=4 6 195 2.0E-10
sp|Q62651|ECH1_RAT Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial OS=Rattus norvegicus GN=Ech1 PE=1 SV=2 17 268 3.0E-10
sp|Q7U004|ECH12_MYCBO Probable enoyl-CoA hydratase echA12 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=echA12 PE=3 SV=1 17 208 4.0E-10
sp|P45361|CRT_PEPDI Short-chain-enoyl-CoA hydratase (Fragment) OS=Peptoclostridium difficile GN=crt PE=3 SV=1 107 261 8.0E-10
sp|Q8BMS1|ECHA_MOUSE Trifunctional enzyme subunit alpha, mitochondrial OS=Mus musculus GN=Hadha PE=1 SV=1 15 226 9.0E-10
sp|Q13825|AUHM_HUMAN Methylglutaconyl-CoA hydratase, mitochondrial OS=Homo sapiens GN=AUH PE=1 SV=1 17 271 9.0E-10
sp|Q64428|ECHA_RAT Trifunctional enzyme subunit alpha, mitochondrial OS=Rattus norvegicus GN=Hadha PE=1 SV=2 15 226 1.0E-09
sp|Q8GYN9|MENB_ARATH 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal OS=Arabidopsis thaliana GN=MENB PE=1 SV=2 2 270 1.0E-09
sp|Q8DSN0|FABM_STRMU Trans-2-decenoyl-[acyl-carrier-protein] isomerase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) GN=fabM PE=3 SV=1 6 271 1.0E-09
sp|Q9JLZ3|AUHM_MOUSE Methylglutaconyl-CoA hydratase, mitochondrial OS=Mus musculus GN=Auh PE=1 SV=1 17 271 2.0E-09
sp|P53526|ECH12_MYCLE Probable enoyl-CoA hydratase echA12 OS=Mycobacterium leprae (strain TN) GN=echA12 PE=3 SV=1 17 179 2.0E-09
sp|O07533|YHAR_BACSU Putative enoyl-CoA hydratase/isomerase YhaR OS=Bacillus subtilis (strain 168) GN=yhaR PE=3 SV=4 14 269 2.0E-09
sp|P9WNN7|ECH12_MYCTU Probable enoyl-CoA hydratase echA12 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=echA12 PE=1 SV=1 17 208 2.0E-09
sp|P9WNN6|ECH12_MYCTO Probable enoyl-CoA hydratase echA12 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=echA12 PE=3 SV=1 17 208 2.0E-09
sp|Q5XIC0|ECI2_RAT Enoyl-CoA delta isomerase 2, mitochondrial OS=Rattus norvegicus GN=Eci2 PE=1 SV=1 7 195 3.0E-09
sp|Q29554|ECHA_PIG Trifunctional enzyme subunit alpha, mitochondrial OS=Sus scrofa GN=HADHA PE=1 SV=1 15 226 2.0E-08
sp|Q54HG7|AUHM_DICDI Methylglutaconyl-CoA hydratase, mitochondrial OS=Dictyostelium discoideum GN=auh PE=3 SV=1 19 271 5.0E-08
sp|A8FP63|FADB_SHESH Fatty acid oxidation complex subunit alpha OS=Shewanella sediminis (strain HAW-EB3) GN=fadB PE=3 SV=1 20 212 6.0E-08
sp|B1KCZ3|FADB_SHEWM Fatty acid oxidation complex subunit alpha OS=Shewanella woodyi (strain ATCC 51908 / MS32) GN=fadB PE=3 SV=1 20 183 9.0E-08
sp|Q49WG8|MENB_STAS1 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) GN=menB PE=3 SV=1 5 269 1.0E-07
sp|B8CH91|FADB_SHEPW Fatty acid oxidation complex subunit alpha OS=Shewanella piezotolerans (strain WP3 / JCM 13877) GN=fadB PE=3 SV=1 20 183 2.0E-07
sp|Q9Y232|CDYL1_HUMAN Chromodomain Y-like protein OS=Homo sapiens GN=CDYL PE=1 SV=2 5 194 2.0E-07
sp|Q6AYK9|CDYL_RAT Chromodomain Y-like protein OS=Rattus norvegicus GN=Cdyl PE=1 SV=1 5 194 3.0E-07
sp|A7MQP0|FADB_CROS8 Fatty acid oxidation complex subunit alpha OS=Cronobacter sakazakii (strain ATCC BAA-894) GN=fadB PE=3 SV=1 29 183 4.0E-07
sp|P24162|ECHH_RHOCB Probable enoyl-CoA hydratase OS=Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) GN=fadB1 PE=3 SV=1 6 271 5.0E-07
sp|P28817|HIBCH_YEAST 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=EHD3 PE=1 SV=2 20 180 6.0E-07
sp|B0TLB9|FADB_SHEHH Fatty acid oxidation complex subunit alpha OS=Shewanella halifaxensis (strain HAW-EB4) GN=fadB PE=3 SV=1 20 183 1.0E-06
sp|Q96DC8|ECHD3_HUMAN Enoyl-CoA hydratase domain-containing protein 3, mitochondrial OS=Homo sapiens GN=ECHDC3 PE=1 SV=2 14 270 1.0E-06
sp|Q8N8U2|CDYL2_HUMAN Chromodomain Y-like protein 2 OS=Homo sapiens GN=CDYL2 PE=1 SV=2 6 237 1.0E-06
sp|Q9D5D8|CDYL2_MOUSE Chromodomain Y-like protein 2 OS=Mus musculus GN=Cdyl2 PE=1 SV=1 6 236 1.0E-06
sp|B5XYH0|FADB_KLEP3 Fatty acid oxidation complex subunit alpha OS=Klebsiella pneumoniae (strain 342) GN=fadB PE=3 SV=1 29 183 2.0E-06
sp|Q8CPQ4|MENB_STAES 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus epidermidis (strain ATCC 12228) GN=menB PE=3 SV=1 5 269 2.0E-06
sp|Q9TM10|MENB_CYACA 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Cyanidium caldarium GN=menB PE=3 SV=1 6 270 2.0E-06
sp|Q5HQC3|MENB_STAEQ 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) GN=menB PE=3 SV=1 5 269 2.0E-06
sp|A8G8D1|FADB_SERP5 Fatty acid oxidation complex subunit alpha OS=Serratia proteamaculans (strain 568) GN=fadB PE=3 SV=1 14 180 3.0E-06
sp|A6TGM4|FADB_KLEP7 Fatty acid oxidation complex subunit alpha OS=Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) GN=fadB PE=3 SV=1 29 183 3.0E-06
sp|A8GYG0|FADB_SHEPA Fatty acid oxidation complex subunit alpha OS=Shewanella pealeana (strain ATCC 700345 / ANG-SQ1) GN=fadB PE=3 SV=1 20 183 3.0E-06
sp|Q3MIE0|ECHD3_RAT Enoyl-CoA hydratase domain-containing protein 3, mitochondrial OS=Rattus norvegicus GN=Echdc3 PE=2 SV=1 12 270 4.0E-06
sp|Q6D2L7|FADJ_PECAS Fatty acid oxidation complex subunit alpha OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) GN=fadJ PE=3 SV=1 25 176 4.0E-06
sp|P9WNP5|MENB_MYCTU 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=menB PE=1 SV=1 3 270 5.0E-06
sp|P9WNP4|MENB_MYCTO 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=menB PE=3 SV=1 3 270 5.0E-06
sp|Q4L549|MENB_STAHJ 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus haemolyticus (strain JCSC1435) GN=menB PE=3 SV=1 5 269 5.0E-06
sp|A0KEL1|FADB_AERHH Fatty acid oxidation complex subunit alpha OS=Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240) GN=fadB PE=3 SV=1 29 182 6.0E-06
sp|Q7MZ92|FADB_PHOLL Fatty acid oxidation complex subunit alpha OS=Photorhabdus luminescens subsp. laumondii (strain TT01) GN=fadB PE=3 SV=1 13 214 7.0E-06
sp|Q7A6A9|MENB_STAAN 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus aureus (strain N315) GN=menB PE=1 SV=1 5 269 7.0E-06
sp|Q99V48|MENB_STAAM 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) GN=menB PE=3 SV=1 5 269 7.0E-06
sp|Q93TU6|CAMK_RHOSO 6-oxocamphor hydrolase OS=Rhodococcus sp. GN=camK PE=1 SV=1 6 179 7.0E-06
sp|A7FDF2|FADB_YERP3 Fatty acid oxidation complex subunit alpha OS=Yersinia pseudotuberculosis serotype O:1b (strain IP 31758) GN=fadB PE=3 SV=1 29 182 9.0E-06
sp|Q66FR8|FADB_YERPS Fatty acid oxidation complex subunit alpha OS=Yersinia pseudotuberculosis serotype I (strain IP32953) GN=fadB PE=3 SV=1 29 182 9.0E-06
sp|B2K0Z6|FADB_YERPB Fatty acid oxidation complex subunit alpha OS=Yersinia pseudotuberculosis serotype IB (strain PB1/+) GN=fadB PE=3 SV=1 29 182 9.0E-06
sp|B1JP63|FADB_YERPY Fatty acid oxidation complex subunit alpha OS=Yersinia pseudotuberculosis serotype O:3 (strain YPIII) GN=fadB PE=3 SV=1 29 182 1.0E-05
sp|A4TR27|FADB_YERPP Fatty acid oxidation complex subunit alpha OS=Yersinia pestis (strain Pestoides F) GN=fadB PE=3 SV=1 29 182 1.0E-05
sp|Q1CN99|FADB_YERPN Fatty acid oxidation complex subunit alpha OS=Yersinia pestis bv. Antiqua (strain Nepal516) GN=fadB PE=3 SV=1 29 182 1.0E-05
sp|A9R754|FADB_YERPG Fatty acid oxidation complex subunit alpha OS=Yersinia pestis bv. Antiqua (strain Angola) GN=fadB PE=3 SV=1 29 182 1.0E-05
sp|Q8ZAN0|FADB_YERPE Fatty acid oxidation complex subunit alpha OS=Yersinia pestis GN=fadB PE=3 SV=1 29 182 1.0E-05
sp|Q1C2C4|FADB_YERPA Fatty acid oxidation complex subunit alpha OS=Yersinia pestis bv. Antiqua (strain Antiqua) GN=fadB PE=3 SV=1 29 182 1.0E-05
sp|A4WFX4|FADB_ENT38 Fatty acid oxidation complex subunit alpha OS=Enterobacter sp. (strain 638) GN=fadB PE=3 SV=1 29 183 1.0E-05
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GO

GO Term Description Terminal node
GO:0003824 catalytic activity Yes
GO:0003674 molecular_function No

SignalP

[Help with interpreting these statistics]
SignalP signal predicted Location
(based on Ymax)
D score
(significance: > 0.45)
No 1 - 63 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|085860
MDYNHYKDISVDRDGPVLTICINRAKRRNTINSNLIEELIHVFGLVDQDDQIRVAILTAEPTAPAFCSGADISGG
WDVLWKPDAEKEGPQAHRDDGGRASIAIYRCRKITISAVNGHAAGAGLTTFQLPFDIRLIWAGAKLTFPFVRRGI
VPEATSSYLLPRLLGHSRANSLILTGETVTPDSPHIRDLYHQILPTRDAVYPAAKALADELAASTSQVSIAFAKG
LLQHPGDSIEENHLLDSKAIKATAGSKDAAEGVKAFFEKRTPKYTGVLSNDLPHWVPWWRRLDIKHLKSKL*
Coding >AgabiH97|085860
ATGGACTACAACCACTACAAGGACATCTCTGTCGACCGCGACGGCCCCGTACTCACCATATGCATTAACCGTGCC
AAACGGCGGAATACCATCAACAGTAACCTCATCGAGGAGCTCATCCATGTCTTTGGGCTCGTCGACCAGGACGAC
CAAATTCGGGTCGCCATTCTCACTGCGGAGCCAACAGCACCCGCATTCTGCTCTGGGGCCGACATTTCTGGTGGT
TGGGATGTACTCTGGAAGCCAGATGCCGAGAAAGAGGGCCCACAAGCCCATAGAGATGATGGCGGCCGTGCCTCC
ATAGCTATCTACCGCTGTCGCAAAATCACCATATCCGCAGTGAATGGCCACGCAGCAGGCGCCGGACTAACGACT
TTCCAACTCCCATTTGACATCCGTCTCATTTGGGCTGGTGCTAAACTCACTTTCCCTTTCGTACGACGCGGTATC
GTTCCTGAAGCTACCTCAAGCTACCTTCTACCTCGACTCCTCGGGCATTCGCGAGCCAATTCTCTGATTCTCACA
GGAGAAACCGTGACTCCGGATTCACCTCACATCCGCGATCTCTACCATCAAATTCTCCCTACACGAGATGCTGTC
TATCCTGCTGCCAAAGCCCTTGCCGATGAACTCGCTGCTAGTACATCTCAGGTTTCAATTGCCTTTGCCAAGGGT
CTCTTACAACACCCCGGGGATAGTATTGAAGAAAACCATCTTCTCGATTCTAAGGCAATCAAGGCCACTGCTGGT
AGCAAAGACGCCGCTGAAGGCGTCAAGGCTTTCTTCGAAAAACGAACACCCAAATATACAGGTGTCCTATCAAAT
GATTTACCTCATTGGGTCCCTTGGTGGCGCAGATTGGACATCAAGCATCTCAAATCCAAACTATAA
Transcript >AgabiH97|085860
ATGGACTACAACCACTACAAGGACATCTCTGTCGACCGCGACGGCCCCGTACTCACCATATGCATTAACCGTGCC
AAACGGCGGAATACCATCAACAGTAACCTCATCGAGGAGCTCATCCATGTCTTTGGGCTCGTCGACCAGGACGAC
CAAATTCGGGTCGCCATTCTCACTGCGGAGCCAACAGCACCCGCATTCTGCTCTGGGGCCGACATTTCTGGTGGT
TGGGATGTACTCTGGAAGCCAGATGCCGAGAAAGAGGGCCCACAAGCCCATAGAGATGATGGCGGCCGTGCCTCC
ATAGCTATCTACCGCTGTCGCAAAATCACCATATCCGCAGTGAATGGCCACGCAGCAGGCGCCGGACTAACGACT
TTCCAACTCCCATTTGACATCCGTCTCATTTGGGCTGGTGCTAAACTCACTTTCCCTTTCGTACGACGCGGTATC
GTTCCTGAAGCTACCTCAAGCTACCTTCTACCTCGACTCCTCGGGCATTCGCGAGCCAATTCTCTGATTCTCACA
GGAGAAACCGTGACTCCGGATTCACCTCACATCCGCGATCTCTACCATCAAATTCTCCCTACACGAGATGCTGTC
TATCCTGCTGCCAAAGCCCTTGCCGATGAACTCGCTGCTAGTACATCTCAGGTTTCAATTGCCTTTGCCAAGGGT
CTCTTACAACACCCCGGGGATAGTATTGAAGAAAACCATCTTCTCGATTCTAAGGCAATCAAGGCCACTGCTGGT
AGCAAAGACGCCGCTGAAGGCGTCAAGGCTTTCTTCGAAAAACGAACACCCAAATATACAGGTGTCCTATCAAAT
GATTTACCTCATTGGGTCCCTTGGTGGCGCAGATTGGACATCAAGCATCTCAAATCCAAACTATAA
Gene >AgabiH97|085860
ATGGACTACAACCACTACAAGGACATCTCTGTCGACCGCGACGGCCCCGTACTCACCATATGCATTAACCGTGCC
AAACGGTAAGCACAATCATCTCCTTCACTCGCCGCACTTCTCCTAACGGCAACCAGGCGGAATACCATCAACAGT
AACCTCATCGAGGAGCTCATCCATGTCTTTGGGCTCGTCGACCAGGACGACCAAATTCGGGTCGCCATTCTCACT
GCGGAGCCAACAGCACCCGCATTCTGCTCTGGGGTAACAATTCTTGCCAATGTTGCACTCAATACTGCTTGCTAA
CTTCTCTCTTTACAGGCCGACATTTCTGGTGGTTGGGATGTACTCTGGAAGCCAGATGCCGAGAAAGAGGGCCCA
CAAGGTAAGAGTATCACCGAGGAATTTTGCCAAGTTTACCAACCCTACTTCCAGCCCATAGAGATGATGGCGGCC
GTGCCTCCATAGCTATCTACCGCTGTCGCAAAATCACCATATCCGCAGTGAATGGCCACGCAGTACGTTCATTTC
ACCTGGGTAGGAATGCTGCTGATTCTTTTGTTGACAGGCAGGCGCCGGACTAACGACTTTCCAACTCCCATTTGA
CATCCGTCTCATTTGGGCTGGTGCTAAACTCACTTTCCCTTTCGTACGACGCGGTATCGTTCCTGAAGGTAAAGC
TCTATCTCATGCCACGAGCCGTGTGACTCATCCTTTGTGTACGACTCAGCTACCTCAAGCTACCTTCTACCTCGA
CTCCTCGGGCATTCGCGAGCCAATTCTCTGATTCTCACAGGAGAAACCGTGACTCCGGATTCACCTCACATCCGC
GATCTCTACCATCAAATTCTCCCTACACGAGATGCTGTCTATCCTGCTGCCAAAGCCCTTGCCGATGAACTCGCT
GCTAGTACATCTCAGGTTTCAATTGCCTTTGCCAAGGGTCTCTTACAACACCCCGGGGATAGTATTGAAGAAAAC
CATCTTCTCGATTCTAAGGCAATCAAGGCCACTGCTGGTAGCAAAGACGCCGCTGAAGGCGTCAAGGCTTTCTTC
GAAAAACGAACACCCAAATATACAGGTGTCCTATCAAATGATTTACCTCATTGGGTCCCTTGGGTGAGCCATGCT
ACGCCCTCATCAGCATTTTTAGATCTCACTTTCGCATGCAGTGGCGCAGATTGGACATCAAGCATCTCAAATCCA
AACTATAA

© 2022 - Robin Ohm - Utrecht University - The Netherlands

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