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Q489W4 (FADA_COLP3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:
3-ketoacyl-CoA thiolase

EC=2.3.1.16
Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Fatty acid oxidation complex subunit beta
Gene names
Name:fadA
Ordered Locus Names:CPS_0392
OrganismColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]
Taxonomic identifier167879 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed By similarity. HAMAP MF_01620

Catalytic activity

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. HAMAP MF_01620

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01620

Subunit structure

Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity.

Subcellular location

Cytoplasm By similarity HAMAP MF_01620.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid degradation
Lipid metabolism
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA C-acyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3863863-ketoacyl-CoA thiolase HAMAP MF_01620
PRO_0000206369

Sites

Active site911Acyl-thioester intermediate By similarity
Active site3421Proton acceptor By similarity
Active site3721Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q489W4 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: E190343259167702

FASTA38640,645
        10         20         30         40         50         60 
MNEVVIVDCI RTPMGRSKAG VFRNVRAEAL SAHLMKQILV RNPALNPEDI EDVIWGCVKQ 

        70         80         90        100        110        120 
TKEQGFNIAR NASLLAGLPK SIGGVTVNRL CGSSMEALHQ ASTSIMSGQG DVFLIGGVEH 

       130        140        150        160        170        180 
MGHVPMMYDV DFDPALNKNI ALASGNMGLT AELLGKQHGI TREMQDAFGA RSHQKAHEAH 

       190        200        210        220        230        240 
LAGRWDNEIV ATQGHDATGA LTLVEHDEVI RPETTAESLS ALRPVFDPVN GTVTAGTSSA 

       250        260        270        280        290        300 
LSDGASAMLV MSAAKAKELG LTPRVKIRGM AVAGCDPATM GFGPVPATKK ALKRAGLSIA 

       310        320        330        340        350        360 
DIELFEFNEA FAAQALSCVR SLKVEDKMDQ INLNGGAIAL GHPLGCSGSR ISGTLINLME 

       370        380 
GQDVNIGLAT MCIGLGQGIA TVFERV 

« Hide

References

[1]"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses."
Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. expand/collapse author list , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed: 16043709] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 34H / ATCC BAA-681.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000083 Genomic DNA. Translation: AAZ25024.1.
RefSeqYP_267150.1. NC_003910.7.

3D structure databases

ProteinModelPortalQ489W4.
SMRQ489W4. Positions 3-386.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ489W4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3518581.
GenomeReviewsGene locus CPS_0392 in contig CP000083_GR.
KEGGcps:CPS_0392.
NMPDRfig|167879.3.peg.450.
PATRIC21464149. VBIColPsy94388_0339.
TIGRCPS_0392.

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHBG370930.
OMAQDAFGAR.
ProtClustDBPRK08947.

Enzyme and pathway databases

BioCycCPSY167879:CPS_0392-MONOMER.

Family and domain databases

HAMAPMF_01620. FadA.
[Tree]
InterProIPR012805. FadA.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.
KOK00632.
PANTHERPTHR18919:SF35. PTHR18919:SF35. 1 hit.
PTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. Thiolase-like. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
TIGR02445. FadA. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADA_COLP3
AccessionPrimary (citable) accession number: Q489W4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 47 of the entry and version 1 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