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Q8FFG4 (FADJ_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. 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:c2886
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length714 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 – 714714Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_0000109300

Regions

Region1 – 190190Enoyl-CoA hydratase By similarity
Region306 – 7144093-hydroxyacyl-CoA dehydrogenase By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q8FFG4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 244CF04A221A6084

FASTA71477,084
        10         20         30         40         50         60 
MEMASAFTLN VRLDNIAVIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK DLRGVVFISA 

        70         80         90        100        110        120 
KPDNFIAGAD INMIANCKTA QEAEALARQG QQLMAEIHAL PVPVIAAIHG ACLGGGLELA 

       130        140        150        160        170        180 
LACHGRVCTD DPKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRAKQAL 

       190        200        210        220        230        240 
KLGLVDDVVP HSILLEAAVE LAKQDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEQKT 

       250        260        270        280        290        300 
QGNYPATKRI LDVIETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRNIFF ASTEVKKDPG 

       310        320        330        340        350        360 
SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLPVRIKDI NPQGINHALK YSWDQLEGKV 

       370        380        390        400        410        420 
RRRHLKASER DKQLALISGT TDYRGFAHRD LIIEAVFENL ELKQQMVAEV EQNCAAHTIF 

       430        440        450        460        470        480 
ASNTSSLPIA DIAAHAARPE QVIGLHFFSP VEKMPLVEII PHAGTSAQTI ATTVKLAKKQ 

       490        500        510        520        530        540 
GKTPIVVRDK AGFYVNRILA PYINEAIRML TEGERVEHID AALVKFGFPV GPIQLLDEVG 

       550        560        570        580        590        600 
IDTGTKIIPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA 

       610        620        630        640        650        660 
IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VRCLDEQVIR SVRDGDIGAV FGIGFPPFLG 

       670        680        690        700        710 
GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCERLVEMSK RGESFWKTTA TDLQ 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the genome structure of the nonpathogenic probiotic Escherichia coli strain Nissle 1917."
Grozdanov L., Raasch C., Schulze J., Sonnenborn U., Gottschalk G., Hacker J., Dobrindt U.
J. Bacteriol. 186:5432-5441(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O6:K5:H1 / Nissle 1917.
[2]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ586889 Genomic DNA. Translation: CAE55846.1.
AE014075 Genomic DNA. Translation: AAN81336.1.
RefSeqNP_754768.1. NC_004431.1.

3D structure databases

ProteinModelPortalQ8FFG4.
SMRQ8FFG4. Positions 1-707.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c2886.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN81336; AAN81336; c2886.
GeneID1038451.
KEGGecc:c2886.
PATRIC18283632. VBIEscCol75197_2723.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000261346.
KOK01782.
OMAPFRYMDT.
OrthoDBEOG6M9F0M.

Enzyme and pathway databases

BioCycECOL199310:C2886-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_ECOL6
AccessionPrimary (citable) accession number: Q8FFG4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 1, 2003
Last modified: June 11, 2014
This is version 87 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