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Q6LTK3 (FADJ_PHOPR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. 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:PBPRA0962
OrganismPhotobacterium profundum (Photobacterium sp. (strain SS9)) [Complete proteome] [HAMAP]
Taxonomic identifier74109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

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_0000109302

Regions

Region8 – 197190Enoyl-CoA hydratase By similarity
Region313 – 7154033-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Site1251Important for catalytic activity By similarity
Site1471Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6LTK3 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: BEDB6D9C220C07A5

FASTA71577,342
        10         20         30         40         50         60 
MTQHESANSQ PSAFSLTFGD NGVAWLKIDV PNERMNTLQS AFVDQVTDVL AQLKDKKDIK 

        70         80         90        100        110        120 
GMVVYSGKPD NFIAGADIRM LAACQTADEA QQLAAKGQEL FGQLEALPFH VVAAIHGPCL 

       130        140        150        160        170        180 
GGGLELALAC HSRVCSDDDK TRLGLPEVQL GLLPGSGGTQ RLPRLIGVAN ALDMILTGKQ 

       190        200        210        220        230        240 
LRAKKAKNLG LVEEAVPLSI LLDIAEKQAL KGKPKRKGSF QEWAMGGNAL GRSVVFDQAA 

       250        260        270        280        290        300 
KKTHEKTRGN YPAADAILDV IKYGLQHGMK KGLDQEAKRF GELVMTSESA ALRSIFFATT 

       310        320        330        340        350        360 
AMKKESGSDA LPATIKKVGV LGGGLMGGGI SHVTATKAGY PVRIKDISND GIKNALVYNF 

       370        380        390        400        410        420 
KLLDKQRKRR IISKAELQNK MFSITGGTTF TGFTNVDVVI EAVFEDINLK HQMVKDIEQQ 

       430        440        450        460        470        480 
TSDYTIFASN TSSLPIHQIA AAAERPENVV GLHYFSPVEK MPLVEVIPHQ GTENGSATSE 

       490        500        510        520        530        540 
QTIATVVALA KKQGKTPIVV ADKAGFYVNR ILAPYMNEAA AVLLSGEPIE HIDRSLLDFG 

       550        560        570        580        590        600 
FPVGPITLLD EVGVDIGAKI SPILLAELGE RFKAPDVFDL LLSDDRKGRK SGKGFYLYNT 

       610        620        630        640        650        660 
KKKEVDKSVY KLLSLEPEQK AAGQDIALRC TLMMLNEAAR CLDEGVIKSA RDGDIGAIFG 

       670        680        690        700        710 
IGFPPFLGGP FRYMDTLGAK RVVEMLKDHT DKYGGRFTPC DKLVAMANEE QSFYS 

« Hide

References

[1]"Life at depth: Photobacterium profundum genome sequence and expression analysis."
Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., Bartlett D.H., Valle G.
Science 307:1459-1461(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SS9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR378666 Genomic DNA. Translation: CAG19373.1.
RefSeqYP_129175.1. NC_006370.1.

3D structure databases

ProteinModelPortalQ6LTK3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING298386.PBPRA0962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG19373; CAG19373; PBPRA0962.
GeneID3125191.
KEGGppr:PBPRA0962.
PATRIC22932665. VBIPhoPro109272_1052.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OMAPFRYMDT.
OrthoDBEOG6M9F0M.

Enzyme and pathway databases

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.
IPR012802. FadJ.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00725. 3HCDH. 1 hit.
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_PHOPR
AccessionPrimary (citable) accession number: Q6LTK3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 76 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