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B5FEW8

- FADB_VIBFM

UniProt

B5FEW8 - FADB_VIBFM

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Protein
Fatty acid oxidation complex subunit alpha
Gene
fadB, VFMJ11_0024
Organism
Vibrio fischeri (strain MJ11)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate By similarity.UniRule annotation

Catalytic activityi

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.UniRule annotation
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.UniRule annotation
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.UniRule annotation
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei119 – 1191Important for catalytic activity By similarity
Sitei139 – 1391Important for catalytic activity By similarity
Binding sitei296 – 2961Substrate By similarity
Binding sitei324 – 3241NAD; via amide nitrogen By similarity
Binding sitei343 – 3431NAD By similarity
Binding sitei407 – 4071NAD By similarity
Active sitei450 – 4501For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding sitei453 – 4531NAD By similarity
Binding sitei500 – 5001Substrate By similarity
Binding sitei660 – 6601Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi400 – 4023NAD By similarity
Nucleotide bindingi427 – 4293NAD By similarity

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-HAMAP
  2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-HAMAP
  3. coenzyme binding Source: InterPro
  4. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-HAMAP
  5. enoyl-CoA hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid degradation, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid oxidation complex subunit alpha
Including the following 2 domains:
Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC:4.2.1.17, EC:5.1.2.3, EC:5.3.3.8)
3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
Gene namesi
Name:fadB
Ordered Locus Names:VFMJ11_0024
OrganismiVibrio fischeri (strain MJ11)
Taxonomic identifieri388396 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
ProteomesiUP000001857: Chromosome I

Subcellular locationi

GO - Cellular componenti

  1. fatty acid beta-oxidation multienzyme complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 725725Fatty acid oxidation complex subunit alphaUniRule annotation
PRO_1000186058Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA) By similarity.

Protein-protein interaction databases

STRINGi388396.VFMJ11_0024.

Structurei

3D structure databases

ProteinModelPortaliB5FEW8.
SMRiB5FEW8. Positions 1-714.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Add
BLAST
Regioni311 – 7254153-hydroxyacyl-CoA dehydrogenase By similarity
Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261344.
KOiK01825.
OMAiAKGMVMQ.
OrthoDBiEOG6M9F0M.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
HAMAPiMF_01621. FadB.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B5FEW8-1 [UniParc]FASTAAdd to Basket

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MIYQGENLSV DYIEPGIAHL VFNAKGSVNK LNLATLQSVG EAIDALYSQK    50
DLQGLLLSSD KSAFIVGADI TEFLGLFDIP TEELSDWLHQ ANAIFNRLED 100
IPVPTLSAIT GFALGGGCEC VLATDFRLAD ETASIGLPET QLGIMPGWGG 150
SVRLPRLIGA DPAMEVITTG KPKRAKDALA LGMIDGVVSR ETLITDSVTM 200
LKKAIGGQLD WQSRRTQKKA PLKLSPLEAA MSFNVAKGMI MKMAGKHYPA 250
PMTAVKSIEN SAFMDRDAAL EVENKNFVAL TQTDVAKSLV GIFLNDQLVK 300
SKAKQAIKNS EPVTSAAVLG AGIMGGGIAY QSASKGVPVL MKDIAQQSLD 350
LGMNEASKLL NKQLERGRLS GLKMAQVLSS ITPSLNYASI ENKDIVVEAV 400
VENPKIKAAV LAEVENEVNE HAILASNTST IPISLLAKSL KRPENFCGMH 450
FFNPVHRMPL VEVIRGEKTS QQTIDRVVAY ASQMGKTPIV VNDCPGFFVN 500
RVLFPYFAGF SLLLRDGGDY QQIDKVMEKE FGWPMGPAYL LDVVGIDTAH 550
HAQAVMAQGF PERMAKNGRD VIDAMFESDR YGQKNGSGFY AYSIDRKGKP 600
KKNIDESTAG IIATVTNTTQ PYTSEQISAR MMIPMINEVI RCLDEGIIAS 650
PAEADMALVY GLGFPPFKGG VFRYLDAIGL TTYLDMAKEF EHLGAVYQVP 700
ESIKQKAADG ECYYPAPQSL SAPSA 725
Length:725
Mass (Da):78,382
Last modified:October 14, 2008 - v1
Checksum:i38CF2E9304DD8549
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001139 Genomic DNA. Translation: ACH65088.1.
RefSeqiYP_002154796.1. NC_011184.1.

Genome annotation databases

EnsemblBacteriaiACH65088; ACH65088; VFMJ11_0024.
GeneIDi6805175.
KEGGivfm:VFMJ11_0024.
PATRICi20118501. VBIVibFis37164_0025.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001139 Genomic DNA. Translation: ACH65088.1 .
RefSeqi YP_002154796.1. NC_011184.1.

3D structure databases

ProteinModelPortali B5FEW8.
SMRi B5FEW8. Positions 1-714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 388396.VFMJ11_0024.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACH65088 ; ACH65088 ; VFMJ11_0024 .
GeneIDi 6805175.
KEGGi vfm:VFMJ11_0024.
PATRICi 20118501. VBIVibFis37164_0025.

Phylogenomic databases

eggNOGi COG1250.
HOGENOMi HOG000261344.
KOi K01825.
OMAi AKGMVMQ.
OrthoDBi EOG6M9F0M.

Enzyme and pathway databases

UniPathwayi UPA00659 .

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
HAMAPi MF_01621. FadB.
InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsi TIGR02437. FadB. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Vibrio fischeri strain MJ11."
    Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.
    Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MJ11.

Entry informationi

Entry nameiFADB_VIBFM
AccessioniPrimary (citable) accession number: B5FEW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 14, 2008
Last modified: June 11, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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