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Q5E3U1 (FADJ_VIBF1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. 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:VF_1810
OrganismVibrio fischeri (strain ATCC 700601 / ES114) [Reference proteome] [HAMAP]
Taxonomic identifier312309 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length687 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.

Sequence caution

The sequence AAW86305.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 687687Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_0000109311

Regions

Region1 – 191191Enoyl-CoA hydratase By similarity
Region307 – 6873813-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Site1191Important for catalytic activity By similarity
Site1411Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5E3U1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 5C85F16B06D6DDC0

FASTA68775,373
        10         20         30         40         50         60 
MKNTSAFAWT KDDEQIAWLT IDVPNEKMNT LQAAFAEQVT QVLDEIEEQQ AHIKGLVIQS 

        70         80         90        100        110        120 
GKPDNFIAGA DINMIANCQN ASEAQALAEK GQHLFQRIED LPFATVAAIH GPCLGGGLEL 

       130        140        150        160        170        180 
ALACDYRVCS DDNKTKLGLP EVQLGLLPGS GGTQRLPRLI GLLPSLDIIL TGKQLRPKTA 

       190        200        210        220        230        240 
LKLGVVDASV PHTILSRIAA DFALKKKAKR KLTAKEWGLS RNPLGRNVIF SQAEKQAQKK 

       250        260        270        280        290        300 
ARGNYPAIAA ILDCIEHGLD KGMKKGLQRE AEQFARLAMT PESAALRSLF FAMTEMKKEK 

       310        320        330        340        350        360 
GSDAEPKSID YVGVLGGGLM GGGIAHVSIA KAKKKVTIKD INNDGLLNAY QYHYQRLDTL 

       370        380        390        400        410        420 
RKRRIISKAQ LQQQMLQLTG VTEFDGFKKL DVVVEAVFED LNLKQEMVKA VQEQGKEDVI 

       430        440        450        460        470        480 
FATNTSSLPI GQIAEGAQKP ENIVGLHYFS PVEKMPLVEV IPHATTSDET ISTVVALAKQ 

       490        500        510        520        530        540 
QGKTPIVVKD SAGFYVNRIL APYMNEAARL LLAGEPIEVL DEALLDFGFP VGPISLLDEV 

       550        560        570        580        590        600 
GVDIGAKIMP ILEAELGDRF RSPDVFQTLI DDKRLGKKTK RGFYVYKGKK KEPDQEVYTL 

       610        620        630        640        650        660 
LNIKPQSQLS KNEIAMRCVL PMLAEAKRCL DEGIIASERD GDIGAIFGIG FPPFLGGPFT 

       670        680 
YMNTLGEEKL ATLMRNYADK YGDRFIE 

« Hide

References

[1]"Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with pathogenic congeners."
Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., Stevens A., Visick K., Whistler C., Greenberg E.P.
Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700601 / ES114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000020 Genomic DNA. Translation: AAW86305.1. Different initiation.
RefSeqYP_205193.1. NC_006840.2.

3D structure databases

ProteinModelPortalQ5E3U1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312309.VF_1810.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW86305; AAW86305; VF_1810.
GeneID3279029.
KEGGvfi:VF_1810.
PATRIC20114314. VBIVibFis127983_1838.

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OMAPFRYMDT.
OrthoDBEOG6M9F0M.

Enzyme and pathway databases

BioCycAFIS312309:GIWP-1914-MONOMER.
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.
IPR018376. Enoyl-CoA_hyd/isom_CS.
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.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADJ_VIBF1
AccessionPrimary (citable) accession number: Q5E3U1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: June 11, 2014
This is version 74 of the entry and version 2 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