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Q5PCX6 (FADJ_SALPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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:SPA0476
OrganismSalmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]
Taxonomic identifier295319 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length715 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 – 715715Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_0000109305

Regions

Region1 – 190190Enoyl-CoA hydratase By similarity
Region306 – 7144093-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Site1181Important for catalytic activity By similarity
Site1401Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PCX6 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 91D34D2066E7B2A4

FASTA71577,235
        10         20         30         40         50         60 
MTTTSAFMLN VRLDNVAVVA IDVPGEKVNT LKAEFAAQVR AILKQIRENK ALQGVVFISA 

        70         80         90        100        110        120 
KADNFIAGAD INIIGHCQNA QEAETLARQG QQLMAEIQAL PVPVIAAIHG ACLGGGLEMA 

       130        140        150        160        170        180 
LACHRRICTD DVKTVLGLPE VQLGLLPGSG GTQRLPRLVG VSTALDMILI GKQLRARQAL 

       190        200        210        220        230        240 
KAGLVDDVVP QTILLEAAVE LAKKERLAQR TLPVRERILA GPLGRALLFR LVRKKTAQKT 

       250        260        270        280        290        300 
QGNYPATERI IDVIETGLAQ GSSSGYDAEA RAFGELAMTP QSQALRAVFF ASTEVKKDPG 

       310        320        330        340        350        360 
SDAPPGPLNS VGILGGGLMG GGIAWVTACK GGLPVRIKDI NTQGINHALK YSWDLLETKV 

       370        380        390        400        410        420 
RRRHIKASER DKQLALISGS TDYRGFSHRD LVIEAVFEDL PLKQQMVAEV EQNCATHTIF 

       430        440        450        460        470        480 
ASNTSSLPIG DIAANAARPE QVIGLHFFSP VEKMPLVEVI PHASTSAQTI ATTVKLAKKQ 

       490        500        510        520        530        540 
GKTPIVVSDK AGFYVNRILA PYINEAIRML TEGERVEHID AALVKFGFPV GPIQLLDEVG 

       550        560        570        580        590        600 
IDTGTKIIPV LEAAYGERFS APANVVASIL NDDRKGRKNG RGFYLYGEKG RKSKKQVDPA 

       610        620        630        640        650        660 
IYKLIGVQGQ SRLSAQQVAE RCVMLMLNEA ARCFDEKVIR SARDGDIGAV FGIGFPPFLG 

       670        680        690        700        710 
GPFRYMDALG PGEMVATLQR LAALYGPRYA PCEQLVRMAE RREHFWTNGE TDQGN 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000026 Genomic DNA. Translation: AAV76478.1.
RefSeqYP_149790.1. NC_006511.1.

3D structure databases

ProteinModelPortalQ5PCX6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295319.SPA0476.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV76478; AAV76478; SPA0476.
PATRIC32350117. VBISalEnt134188_0508.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
OMAMMLNEAA.
OrthoDBEOG6M9F0M.
ProtClustDBPRK11154.

Enzyme and pathway databases

BioCycSENT295319:GJBZ-475-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.
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.
TIGRFAMsTIGR02440. FadJ. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADJ_SALPA
AccessionPrimary (citable) accession number: Q5PCX6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 67 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