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Q87MM3 (FADJ_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid oxidation complex subunit alpha

Including the following 2 domains:

  1. Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase
    EC=4.2.1.17
    EC=5.1.2.3
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:fadJ
Ordered Locus Names:VP2208
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length703 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities By similarity. HAMAP-Rule MF_01617

Catalytic activity

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. HAMAP-Rule MF_01617

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. HAMAP-Rule MF_01617

(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP-Rule MF_01617

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP-Rule MF_01617

Subunit structure

Heterotetramer of two alpha chains (FadJ) and two beta chains (FadI) By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01617.

Sequence similarities

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

In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid degradation
Lipid metabolism
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionIsomerase
Lyase
Oxidoreductase
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-hydroxyacyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

3-hydroxybutyryl-CoA epimerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

NAD binding

Inferred from electronic annotation. Source: InterPro

enoyl-CoA hydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 703703Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_0000109312

Regions

Region1 – 190190Enoyl-CoA hydratase By similarity
Region308 – 7033963-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Site1181Important for catalytic activity By similarity
Site1401Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87MM3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: A2A62EDC4047BA3F

FASTA70376,856
        10         20         30         40         50         60 
MSEQKAFSLN VDEQNIAWLA IDVPNEKMNT LQAAFADEMK EIFAQLKDSS GIKGMIIHSL 

        70         80         90        100        110        120 
KPDNFVAGAD VRMLEACTTA NEAQALAKQG QELFQQLSDL PYPVVAAIHG PCLGGGLELA 

       130        140        150        160        170        180 
LACDYRVCTD FDKTRLGLPE VQLGLLPGSG GTQRLPRLIG LLPSLDLILT GKQLRAKKAK 

       190        200        210        220        230        240 
KLGVVDACVP DTILLDVAKQ FIDKGKNKGK KKQSTKEKLM SGSGLGRKLV FEQAAKKTNQ 

       250        260        270        280        290        300 
KTRGNYPATV AILEVIQHGL EKGFAQGQEL EAKRFGELVM SSESKALRSI FFATTEMKKE 

       310        320        330        340        350        360 
HGTDAQPAAV KKVGVLGGGL MGAGISHVTV AKAKVPVRIK DVSNDGVLNA LNYNYKLFEK 

       370        380        390        400        410        420 
QRKRRILSKA DLQAKMLQLS GGVDFTSYNH IDVVIEAVFE DLDLKQQMVA DIEANAKSET 

       430        440        450        460        470        480 
IFATNTSSLP IHKIAEKAER PENIVGLHYF SPVEKMPLVE VIPHETTSDE TISTVVALAK 

       490        500        510        520        530        540 
KQGKTPIVVK DKAGFYVNRI LAPYMNEAAH ILLANEPIEK LDGALLDFGF PVGPITLLDE 

       550        560        570        580        590        600 
VGVDIGAKIM PILVNELGER FKGPDVFDIL LNDGRKGRKS GKGFYTYKGK KKEVDKSIYK 

       610        620        630        640        650        660 
LLKLTPESKL SDNDIALRCV LPMLNEAVRC LDDGIIRSPR DGDIGAIFGI GFPPFLGGPF 

       670        680        690        700 
RYMDQFGLKE LVEKMNEFAS KYGDRYAPCD GLLTRAGEGR TFY 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC60471.1.
RefSeqNP_798587.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87MM3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP2208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC60471; BAC60471; BAC60471.
GeneID1189721.
KEGGvpa:VP2208.
PATRIC20142564. VBIVibPar50997_2111.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OMAPFRYMDT.
OrthoDBEOG6M9F0M.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-2265-MONOMER.
UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
HAMAPMF_01617. FadJ.
InterProIPR006180. 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.
IPR012802. FadJ.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsTIGR02440. FadJ. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADJ_VIBPA
AccessionPrimary (citable) accession number: Q87MM3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: June 1, 2003
Last modified: June 11, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways