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A8ADP2 (FADJ_CITK8) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 50. 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:CKO_00449
OrganismCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) [Complete proteome] [HAMAP]
Taxonomic identifier290338 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter

Protein attributes

Sequence length715 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 – 715715Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_1000069482

Regions

Region1 – 190190Enoyl-CoA hydratase By similarity
Region306 – 7154103-hydroxyacyl-CoA dehydrogenase By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A8ADP2 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: FFB62A3590FB4A32

FASTA71577,162
        10         20         30         40         50         60 
MDMTSAFTLN VRLDNVAVVS IDVPGEKMNT LKAEFATQVR AILKQIRENK ALRGVVFISA 

        70         80         90        100        110        120 
KPDNFIAGAD INMIGNCKSA QEAETLARQG QQIMAEIQAL SVPVVAAIHG ACLGGGLEMA 

       130        140        150        160        170        180 
LACHRRICTD DAKTVLGLPE VQLGLLPGSG GTQRLPRLVG VSTALDMILT GKQLRPKQAL 

       190        200        210        220        230        240 
RVGLVDEVVP HAILLEAAVE LAIKGRSAQR NLPVRERILA GPLGRTLLFR MVSKKTGQKT 

       250        260        270        280        290        300 
QGNYPATERI LEVIETGLAQ GSSSGYDAEA RAFGELAMTP QSQALRNIFF ASTEVKKDPG 

       310        320        330        340        350        360 
SDAQPGPLAS VGVLGGGLMG GGIAYVTACK GGLSVRIKDI NAKGINHALK YSWDQLETKV 

       370        380        390        400        410        420 
RRRHIKAGER DKQLALISGS TDYRGFSHRD LVIEAVFEDL ALKQQMVAEV EQNCAPHTIF 

       430        440        450        460        470        480 
ASNTSSLPIG DIAANAARPE QVIGLHFFSP VEKMPLVEVI PHATTSAQTI ATTVKLAKKQ 

       490        500        510        520        530        540 
GKTPIVVSDK AGFYVNRILA PYINEAIRLL TEGERVEAID AALVKFGFPV GPIQLLDEVG 

       550        560        570        580        590        600 
IDTGTKIIPV LEAAYGERFS APANVVASIL NDDRKGRKNG RGFYLYGVKG RKSKKQVDPA 

       610        620        630        640        650        660 
IYRLIGTQGQ SRLSAQQMAE RCVMLMLNEA ARCFDEKVIR SARDGDIGAV FGIGFPPFLG 

       670        680        690        700        710 
GPFRYMDTLG AGEVVAVLQR LATQYGDRFT PCERLLRMAE RGERFWNSGE TDLKE 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000822 Genomic DNA. Translation: ABV11605.1.
RefSeqYP_001452041.1. NC_009792.1.

3D structure databases

ProteinModelPortalA8ADP2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290338.CKO_00449.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV11605; ABV11605; CKO_00449.
GeneID5581769.
KEGGcko:CKO_00449.
PATRIC20384294. VBICitKos71230_0378.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OMAPFRYMDT.
OrthoDBEOG6M9F0M.

Enzyme and pathway databases

BioCycCKOS290338:GJ8L-449-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_CITK8
AccessionPrimary (citable) accession number: A8ADP2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: June 11, 2014
This is version 50 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