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Q9KT58 (FADJ_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:VC_1047
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

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.

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 AAF94206.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 708708Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_0000109310

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
Q9KT58 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 8CFFF5EA8E1FE3F7

FASTA70877,357
        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 KLLANTDLGR 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003852 Genomic DNA. Translation: AAF94206.1. Different initiation.
PIRF82248.
RefSeqNP_230692.2. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KT58.
ModBaseSearch...

Protein-protein interaction databases

STRING243277.VC1047.

Protocols and materials databases

DNASU2614317.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF94206; AAF94206; VC_1047.
GeneID2614317.
KEGGvch:VC1047.
PATRIC20081192. VBIVibCho83274_0999.

Phylogenomic databases

eggNOGCOG1250.
KOK01782.
OMASPKRDKG.
ProtClustDBPRK11154.

Enzyme and pathway databases

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. 6DGDH_C_like. 2 hits.
TIGRFAMsTIGR02440. FadJ. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADJ_VIBCH
AccessionPrimary (citable) accession number: Q9KT58
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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