Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6D2L7 (FADJ_PECAS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. 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:ECA3078
OrganismPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica) [Complete proteome] [HAMAP]
Taxonomic identifier218491 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

Protein attributes

Sequence length731 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 – 731731Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_0000109297

Regions

Region15 – 204190Enoyl-CoA hydratase By similarity
Region320 – 7294103-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Site1321Important for catalytic activity By similarity
Site1541Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6D2L7 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: DAAB4DA0B42ECCB3

FASTA73180,047
        10         20         30         40         50         60 
MNDQQPFSVT ASPTTEKTSA FSLTIRPDNI GVISIDVPGE RVNTLKSEFA EQILSVFELA 

        70         80         90        100        110        120 
RQHATLRGLI FISAKPDSFI AGADITMLNK CSSAEQAENL AKQGQETFDQ IAALPFPVVA 

       130        140        150        160        170        180 
AIHGACLGGG LELALACDYR VCSLDEKTVL GLPEVQLGLL PGSGGTQRLP RLIGLDSALD 

       190        200        210        220        230        240 
LILTGRHLRA GQALRQGLVD EAVPHDILLD TAVEILKKGK RKAVPLGWRS RLLNSPGIRH 

       250        260        270        280        290        300 
LLFKMVKRKT RAKTHGNYPA TEKIIQVVRR GIEKGREEGY RHEARAFGKL VMTPESAALR 

       310        320        330        340        350        360 
HLFFATNALK KTSGAASEAK PIHRVGILGG GLMGGGIASV TATRGQLPVR IKDINEQGIN 

       370        380        390        400        410        420 
HALKYNWQLL TKRVQSKRMK PTERQRLMTL ISGSTDYRGF EHADIVIEAV FEDLALKRQM 

       430        440        450        460        470        480 
ITEIEDHAAP HTIFASNTSS LPIHQIAEGA RRPQLVVGLH YFSPVDKMPL VEVIPHAHTS 

       490        500        510        520        530        540 
AETVATTVAL ARKQGKTAIV VGDSAGFYVN RILAPYINEA AYCLLEGEPI ESIDYALVRF 

       550        560        570        580        590        600 
GFPVGPLALL DEVGIDVATK IVPVLSEELG DRFTSPPAFD AILKDGRKGR KNGKGFYRYN 

       610        620        630        640        650        660 
KTRRFWHSGK EVDSSVYPLL DVTPKAHIDP ALISQRAVMM MLNEAARCLD EGVIQCARDG 

       670        680        690        700        710        720 
DIGAVFGIGF PPFLGGPFHY MDRLGMETVV KTLLVLQQQY GDRFAPCERL LTMREGQRTF 

       730 
YPPADKDNSI S 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950851 Genomic DNA. Translation: CAG75977.1.
RefSeqYP_051168.1. NC_004547.2.

3D structure databases

ProteinModelPortalQ6D2L7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218491.ECA3078.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG75977; CAG75977; ECA3078.
GeneID2883878.
KEGGeca:ECA3078.
PATRIC20481467. VBIPecAtr54885_3111.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OMAMMLNEAA.
OrthoDBEOG6M9F0M.
ProtClustDBPRK11154.

Enzyme and pathway databases

BioCycPATR218491:GJNB-3126-MONOMER.
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.
IPR018376. Enoyl-CoA_hyd/isom_CS.
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.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADJ_PECAS
AccessionPrimary (citable) accession number: Q6D2L7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 75 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