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A8GH86 (FADJ_SERP5) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 51. 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:Spro_3378
OrganismSerratia proteamaculans (strain 568) [Complete proteome] [HAMAP]
Taxonomic identifier399741 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

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.

Sequence caution

The sequence ABV42476.1 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 – 715715Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_0000335591

Regions

Region1 – 194194Enoyl-CoA hydratase By similarity
Region310 – 7154063-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Site1221Important for catalytic activity By similarity
Site1441Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A8GH86 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: A39FA88CFF8406A5

FASTA71577,439
        10         20         30         40         50         60 
MHEQRAKPSA FQLTIRPDNI GVITIDVPGE KVNTLKAEFV EQVNDVLIRA QQHPALEGLV 

        70         80         90        100        110        120 
IVSGKPDSFI AGADITMIAA CTTAKEAETL AKKGQSTLAQ IAAFQVPVVA AIHGACLGGG 

       130        140        150        160        170        180 
LELALACHGR VCSLDDKTAL GLPEVQLGLL PGSGGTQRLP RLIGASKALD MILTGKHIRA 

       190        200        210        220        230        240 
RQALRLGLVD DAVPQSILLQ TAIERVKQGW QSRRELPWQE RLLNGPLGKS LLFSIVRKKT 

       250        260        270        280        290        300 
LAKTHGNYPA AERIIQVVRT GLDSGIASGY EAEARAFGEL AMTPQSAALR SLFFASTALK 

       310        320        330        340        350        360 
KERGGNAQPH ALHRIGILGG GLMGGGIACV TATRGGLPVR IKDVNETGIN HALKYSWDVL 

       370        380        390        400        410        420 
SKRVRSKRMR PAERQKQMML ISGSTDYSGF DQVDVVIEAV FEDLSLKQQM VAEIEQHAAP 

       430        440        450        460        470        480 
HTIFASNTSS LPIGQIAAKA QRPEQVIGLH YFSPVDKMPL VEVIPHATTS EETIATTVAL 

       490        500        510        520        530        540 
AHKQGKTAIV VADRAGFYVN RILAPYINEA ARCLLEGEPI ESLDKALVDF GFPVGPITLL 

       550        560        570        580        590        600 
DEVGIDVGTK ISPVLVEQLG PRFAAPAAFD AVLKDGRKGR KNGRGFYLYP SEGQQRQRHK 

       610        620        630        640        650        660 
RADTSVYILL GITPKSHLQQ AVIAQRCVMM MLNEAARCLD EGVIRSARDG DIGAVFGIGF 

       670        680        690        700        710 
PPFLGGPFRY MDQLGVEKVV KTLEYLQRQH GEYFAPCERL QRMAQQGERF YPQGS 

« Hide

References

[1]"Complete sequence of chromosome of Serratia proteamaculans 568."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 568.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000826 Genomic DNA. Translation: ABV42476.1. Different initiation.
RefSeqYP_001479604.1. NC_009832.1.

3D structure databases

ProteinModelPortalA8GH86.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399741.Spro_3378.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV42476; ABV42476; Spro_3378.
GeneID5603340.
KEGGspe:Spro_3378.
PATRIC32419542. VBISerPro44537_3435.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OrthoDBEOG6M9F0M.

Enzyme and pathway databases

BioCycSPRO399741:GI55-3446-MONOMER.
UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 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.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADJ_SERP5
AccessionPrimary (citable) accession number: A8GH86
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 51 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