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A5F2P2 (FADJ_VIBC3) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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:VC0395_A0565, VC395_1061
OrganismVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) [Complete proteome] [HAMAP]
Taxonomic identifier345073 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length708 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 ACP09073.1 differs from that shown. Reason: Erroneous initiation.

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 – 708708Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_1000073632

Regions

Region1 – 191191Enoyl-CoA hydratase By similarity
Region311 – 7083983-hydroxyacyl-CoA dehydrogenase By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A5F2P2 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 77AD9F2EDDA527A4

FASTA70877,299
        10         20         30         40         50         60 
MDNNNAFQLS FDEQHYAWLA IDVPGEKMNT LQAAFAEEMQ AVFATLNEKR GQIKGLIIHS 

        70         80         90        100        110        120 
LKPDNFIAGA DVRMLEACQS VHEAQALASQ GQQMFQQLAD LPFPVVAAIH GPCLGGGLEL 

       130        140        150        160        170        180 
ALACDYRVCT EDEVTRLGLP EVMLGLLPGS GGTQRLPRLI GLLPALDLIL TGKQLRAKKA 

       190        200        210        220        230        240 
KKLGVVDACV PHSVLLDVAK RLLEEKGHKK RAQVTLPIKE KLLANTGLGR KLIFDQAAKK 

       250        260        270        280        290        300 
TQQKTRGNYP AAQAILEVIQ YGLEKGMHAG LEYEAKRFAE LVMTRESKAL RSIFFATTEM 

       310        320        330        340        350        360 
KKDLGADAKP APVAAVGVLG GGLMGAGISH VTVAKAKTSV RIKDVANDGV LNALNYNYKL 

       370        380        390        400        410        420 
FDKQRQRKIL TKAQLQAQMS QLSGGTGFVG FDRCDVVIEA VFEDLKLKQQ MVADIEANAK 

       430        440        450        460        470        480 
PTTIFATNTS SLPIHQIASQ AQRPQNIVGL HYFSPVEKMP LVEVIPHATT SDETIATVVT 

       490        500        510        520        530        540 
LARKQGKTPI VVKDCAGFYV NRILAPYMNE AAQVLMAGEP IEKLDAALLD FGFPVGPITL 

       550        560        570        580        590        600 
LDEVGVDIGA KIMPILVKEL GPRFQGPDVF DVLLKDNRKG RKSGKGFYTY KGSKKKEVDK 

       610        620        630        640        650        660 
SVYKLLKLTP ESKLNDKEIA MRCLLPMLNE AVRCLDEGII RSARDGDMGA IFGIGFPPFL 

       670        680        690        700 
GGPFRYMDTL GLTKVVEMMN QHTEKYGERF APCDGLLTRA GLGEKFYP 

« Hide

References

[1]Heidelberg J.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395.
[2]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000627 Genomic DNA. Translation: ABQ20084.1.
CP001235 Genomic DNA. Translation: ACP09073.1. Different initiation.
RefSeqYP_001216515.1. NC_009457.1.
YP_002819309.1. NC_012582.1.

3D structure databases

ProteinModelPortalA5F2P2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING345073.VC0395_A0565.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ20084; ABQ20084; VC0395_A0565.
ACP09073; ACP09073; VC395_1061.
GeneID5135643.
7776825.
KEGGvco:VC0395_A0565.
vcr:VC395_1061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OMAPFRYMDT.

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.
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.
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_VIBC3
AccessionPrimary (citable) accession number: A5F2P2
Secondary accession number(s): C3LZ57
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 12, 2007
Last modified: June 11, 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