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A1RI92 (FADJ_SHESW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:Sputw3181_1549
OrganismShewanella sp. (strain W3-18-1) [Complete proteome] [HAMAP]
Taxonomic identifier351745 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length706 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 – 706706Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_0000323531

Regions

Region1 – 188188Enoyl-CoA hydratase By similarity
Region308 – 7063993-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Site1161Important for catalytic activity By similarity
Site1381Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A1RI92 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: C7147BBF7BCC18C4

FASTA70675,958
        10         20         30         40         50         60 
MEKTFNLTRR DDGIAILTMD VPGETMNTLK AQFGPEISEI LAEIKSDPHI RGLVLISGKK 

        70         80         90        100        110        120 
DSFVAGADIS MLDACKTAGD AKALSQQGHV VFNELEALKI PVVAAIHGAC LGGGLELALA 

       130        140        150        160        170        180 
CHQRVCSDDG KTMLGVPEVQ LGLLPGGGGT QRLPRLVGIT TALDMMLTGK QIRSKQALKM 

       190        200        210        220        230        240 
GLVNDVVPQT ILLQTAVEMA LTGKRAPKPV KKSLVNQVLE GTSFGRNIIF DQATKQVEKK 

       250        260        270        280        290        300 
TQGNYPAPAK IIDCVRQGIA KGMQKGLEVE ASHFAELVVS KESEALRSIF FATTEMKKET 

       310        320        330        340        350        360 
GAEGATPRKV KKAVILGGGL MGGGIASVTT TKAKIPVRVK DISEKGLSNA LAYAYKLLDK 

       370        380        390        400        410        420 
GVKRRHMTPA ARDNLMALMT TTTEYKGVKD ADIIVEAVFE DLALKHQMVK DIERECGEHT 

       430        440        450        460        470        480 
IFASNTSSLP ISQIAEAATR PENVIGLHYF SPVEKMPLVE VIAHAKTSPE TIATTVAFAR 

       490        500        510        520        530        540 
KQGKTPIVVQ DGAGFYVNRI LALYMNEAAQ LLLEGQSVEH LDKALVKFGF PVGPITLLDE 

       550        560        570        580        590        600 
VGIDVGAKIS PILEKELGER FKAPAAFDKL LGDDRKGRKN GKGFYQYGAS SKKTKAVDET 

       610        620        630        640        650        660 
VYGVLGIKPG TNKDAKALAE RCVVQMLNEA VRCLDDGIIA SPRDGDIGAI FGIGFPPFLG 

       670        680        690        700 
GPFHYIDTLG AANLVKILES YQSQFGNRFE PCERLKTMAR ENVSFF 

« Hide

References

[1]"Complete sequence of Shewanella sp. W3-18-1."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: W3-18-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000503 Genomic DNA. Translation: ABM24387.1.
RefSeqYP_962941.1. NC_008750.1.

3D structure databases

ProteinModelPortalA1RI92.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351745.Sputw3181_1549.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM24387; ABM24387; Sputw3181_1549.
GeneID4658154.
KEGGshw:Sputw3181_1549.
PATRIC23596689. VBISheSp103602_1611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSP351745:GCOY-1606-MONOMER.
UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
HAMAPMF_01617. FadJ.
InterProIPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
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.
TIGRFAMsTIGR02440. FadJ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFADJ_SHESW
AccessionPrimary (citable) accession number: A1RI92
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 57 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