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A4TM82 (FADJ_YERPP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 59. 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:YPDSF_2013
OrganismYersinia pestis (strain Pestoides F) [Complete proteome] [HAMAP]
Taxonomic identifier386656 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length774 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 – 774774Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_0000323533

Regions

Region1 – 224224Enoyl-CoA hydratase By similarity
Region340 – 7744353-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Site1521Important for catalytic activity By similarity
Site1741Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A4TM82 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: D10D346111BFD403

FASTA77483,594
        10         20         30         40         50         60 
MSKENIVTRE NTAVSENAVS EPTVNNDVGA SATNSVTHPA FTLNVRPDNI GIITIDVVGD 

        70         80         90        100        110        120 
KVNTLKAEFA DQIATILQQA HALPKLQGLV IVSGKPDSFI AGADITMIAA CRTAHDARVL 

       130        140        150        160        170        180 
AQKGQSILAQ IAAFPVPVVA AIHGACLGGG LELALACHSR ICSLDDKTVL GLPEVQLGLL 

       190        200        210        220        230        240 
PGSGGTQRLP RLVGVSKALD MILTGKQIRP RQALKMGLVD DVVPRDILLD VAIQRAKAGW 

       250        260        270        280        290        300 
LNRRALPWQE RLLSGPLGKA LLFRIVRKKT LAKTRGHYPA AERIIDVVRK GLDQGGPSGY 

       310        320        330        340        350        360 
EAEARAFGEL AMSPQSAALR SLFFATTSLK KETGSAATAR AIHRVGVLGG GLMGGGIANV 

       370        380        390        400        410        420 
TATRAGLPVR IKDINPQGIN QALKYTWDAL GKRVRSKRMR PTEQQRQMML ISGSTDYRGF 

       430        440        450        460        470        480 
ERVDIVVEAV FEDLSLKQQM VADIERFGAA HTIFASNTSS LPISQIAALA QRPEQVIGLH 

       490        500        510        520        530        540 
YFSPVDKMPL VEVIPHEKTS EETIATTVAL ARKQGKTAIV VADRAGFYVN RILAPYINEA 

       550        560        570        580        590        600 
ARCLLDGEPI ESVDNALVDF GFPVGPMMLL DEVGIDVATK IMPILVEQLG PRFAAPPSFD 

       610        620        630        640        650        660 
VILKDGRKGR KNGRGFYLYS NPTKNSSPTK NGNSPAKRNS FKWRKNKVKP VDASIYTLLG 

       670        680        690        700        710        720 
VTPKAHLGAG VITQRCTMLM LNEAVRCLDE SIIRNPRDGD IGAVFGIGFP PFLGGPFRYL 

       730        740        750        760        770 
DSLGADKVVQ ALRLLVQQYG ERFEPCQRLV TMAEQQQQFY PVDANIDEVT DVAS 

« Hide

References

[1]"Complete sequence of chromosome of Yersinia pestis Pestoides F."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pestoides F.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000668 Genomic DNA. Translation: ABP40394.1.
RefSeqYP_001163367.1. NC_009381.1.

3D structure databases

ProteinModelPortalA4TM82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING386656.YPDSF_2013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP40394; ABP40394; YPDSF_2013.
GeneID5065641.
KEGGypp:YPDSF_2013.
PATRIC18613436. VBIYerPes122972_2620.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OMAPFRYMDT.
OrthoDBEOG6M9F0M.

Enzyme and pathway databases

BioCycYPES386656:GKD7-2049-MONOMER.
UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 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.
IPR029045. ClpP/crotonase-like_dom.
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.
SSF52096. SSF52096. 1 hit.
TIGRFAMsTIGR02440. FadJ. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADJ_YERPP
AccessionPrimary (citable) accession number: A4TM82
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 15, 2007
Last modified: June 11, 2014
This is version 59 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