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A1JK30 (FADJ_YERE8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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
Synonyms:faoA
Ordered Locus Names:YE1277
OrganismYersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) [Complete proteome] [HAMAP]
Taxonomic identifier393305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length745 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.

Sequence caution

The sequence CAL11369.1 differs from that shown. Reason: Erroneous initiation.

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 – 745745Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_0000323532

Regions

Region47 – 209163Enoyl-CoA hydratase By similarity
Region325 – 7454213-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Site1371Important for catalytic activity By similarity
Site1591Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A1JK30 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: B31E7B68E3F51798

FASTA74579,924
        10         20         30         40         50         60 
MSQENTLNSG DETILAEAVA PAHAVFTLSV RPDNIGIITV DVVGDKVNTL KAKFAEQIAE 

        70         80         90        100        110        120 
ILQQAQALSQ LQGLVIISGK PDSFIAGADI TMIAACHTAQ DARILAQKGQ SILAQIAAFP 

       130        140        150        160        170        180 
VPVVAAIHGA CLGGGLELAL ACHSRICSQD DKTVLGLPEV QLGLLPGSGG TQRLPRLVGV 

       190        200        210        220        230        240 
SKALDMILTG RQVRARQALK MGLVDDVVPQ DILLDVAIQR AKAGWLDKPA LPWQERLLSG 

       250        260        270        280        290        300 
PLGKALLFNI VRKKTQAKTK GHYPAAERII DVVRKGLDHG GPAGYEAEAK AFGELAMTPE 

       310        320        330        340        350        360 
SAALRSLFFA TTSLKKESGG KAQPRAIHRV GVLGGGLMGG GIANVTATRA GLPVRIKDIN 

       370        380        390        400        410        420 
PTGINQALKY TWDTLGKRVR SKRMRPAERQ RQMMLISGST DYCGFGNVDI VVEAVFEDLS 

       430        440        450        460        470        480 
LKQQMVADIE HFAAPHTIFA SNTSSLPISD IAAQAQRPEQ VIGLHYFSPV DKMPLVEVIP 

       490        500        510        520        530        540 
HAKTSEETIA TTVALARKQG KTAIVVADRA GFYVNRILAP YINEAARCLL DGEPIASVDK 

       550        560        570        580        590        600 
ALVDFGFPVG PITLLDEVGI DVGTKIIPIL VEKLGARFAA PPSFDVILKD GRKGRKNGRG 

       610        620        630        640        650        660 
FYLYPAKSSG FKWKRSPVKQ VDTSVYTLLG VTPKAHLESA VIAQRCTMMM LNEAARCLDE 

       670        680        690        700        710        720 
SIIRNPRDGD IGAVFGIGFP PFLGGPFRYM DSLGADKVVK TLNLLAQQYG ERFEPCSLLV 

       730        740 
TMAGQQKRFY PPENSLDEAA ITAHN 

« Hide

References

[1]"The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081."
Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. expand/collapse author list , Quail M.A., Dougan G., Parkhill J., Prentice M.B.
PLoS Genet. 2:2039-2051(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 13174 / 8081.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286415 Genomic DNA. Translation: CAL11369.1. Different initiation.
RefSeqYP_001005598.1. NC_008800.1.

3D structure databases

ProteinModelPortalA1JK30.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393305.YE1277.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL11369; CAL11369; YE1277.
GeneID4715636.
KEGGyen:YE1277.
PATRIC18562028. VBIYerEnt11519_1387.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OrthoDBEOG6M9F0M.
ProtClustDBPRK11154.

Enzyme and pathway databases

UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
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.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
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.
TIGRFAMsTIGR02440. FadJ. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADJ_YERE8
AccessionPrimary (citable) accession number: A1JK30
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: February 19, 2014
This is version 56 of the entry and version 2 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