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B5R3R9 (FADJ_SALEP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:SEN2370
OrganismSalmonella enteritidis PT4 (strain P125109) [Complete proteome] [HAMAP]
Taxonomic identifier550537 [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_1000185949

Regions

Region1 – 190190Enoyl-CoA hydratase By similarity
Region306 – 7154103-hydroxyacyl-CoA dehydrogenase By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
B5R3R9 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: B75AB97AB9A67A93

FASTA71577,238
        10         20         30         40         50         60 
MTTTSAFMLN VRLDNVAVVA IDVPGEKVNT LKAEFAAQVR AILKQIRENK ALQGVVFISA 

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

       130        140        150        160        170        180 
LACHRRICTD DVKTVLGLPE VQLGLLPGSG GTQRLPRLVG VSTALDMILT 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 
RRRHIKANER DKQLALISGS TDYRGFSHRD LVIEAVFEDL PLKQQMVAEV EQNCAAHTIF 

       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]"Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways."
Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. expand/collapse author list , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.
Genome Res. 18:1624-1637(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: P125109.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM933172 Genomic DNA. Translation: CAR33954.1.
RefSeqYP_002244457.1. NC_011294.1.

3D structure databases

ProteinModelPortalB5R3R9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING550537.SEN2370.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC32335269. VBISalEnt14964_2408.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
OMAMMLNEAA.
OrthoDBEOG6M9F0M.
ProtClustDBPRK11154.

Enzyme and pathway databases

BioCycSENT550537:GJFI-2399-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_SALEP
AccessionPrimary (citable) accession number: B5R3R9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 4, 2008
Last modified: February 19, 2014
This is version 45 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