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Reviewed, UniProtKB/Swiss-Prot Q8ZAM9 (FADA_YERPE)

Last modified February 9, 2010. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-ketoacyl-CoA thiolase
    EC=2.3.1.16
Alternative name(s):
    Fatty acid oxidation complex subunit beta
    Beta-ketothiolase
    Acetyl-CoA acyltransferase
Gene names
Name: fadA
Ordered Locus Names: YPO3767, y0463, YP_3281
OrganismYersinia pestis [Complete proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length387 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. Involved in the aerobic and anaerobic degradation of long-chain fatty acids 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. HAMAP MF_01620

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: HAMAP

lipid catabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA C-acyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3873873-ketoacyl-CoA thiolase HAMAP MF_01620
PRO_0000206400

Sites

Active site911Acyl-thioester intermediate By similarity
Active site3431Proton acceptor By similarity
Active site3731Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZAM9-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 1690502C07AE9F63

FASTA38740,917
        10         20         30         40         50         60 
MENVVIIDAV RTPMGRSKGG AFRHVRAEDL SAHLMRAVIS RNPGLNAAEI DDIYWGCVQQ 

        70         80         90        100        110        120 
TLEQGFNIAR NASLLAEIPH SVPAVTVNRL CGSSMQALHD GARAIMVGDA KISLIGGVEH 

       130        140        150        160        170        180 
MGHVPMNHGV DFHPGMGRTV AKAAGMMGLT AEMLAKIHNI SRQSQDEFAF RSHQRAYAAT 

       190        200        210        220        230        240 
QAGHFAKEIV ATNGHDAEGV LKRFDFDEVI RPETNLSGLA ALRPAFDPVN GTVTAGTSSA 

       250        260        270        280        290        300 
LSDGASAMLI MSESRAKSLG LTPRARIRSM AVVGCDPSIM GYGPVPASQL ALKRAGLELA 

       310        320        330        340        350        360 
DIGLFELNEA FAAQSLACLK GLGLLESMDD KVNLNGGAIA LGHPLGCSGA RISTTLLNLM 

       370        380 
ERRDVQFGLA TMCIGLGQGI ATVFERL 

« Hide

References

[1]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed: 11586360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed: 12142430] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM5 / Biovar Mediaevalis.
[3]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed: 15368893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590842 Genomic DNA. Translation: CAL22354.1.
AE009952 Genomic DNA. Translation: AAM84052.1.
AE017042 Genomic DNA. Translation: AAS63448.1.
PIRAG0458.
RefSeqNP_667801.1.
NP_994571.1.
YP_002348646.1.

3D structure databases

SMRQ8ZAM9. Positions 3-387.
ModBaseSearch...

Genome annotation databases

GeneID1145410.
1176602.
2763243.
GenomeReviewsGene locus y0463 in contig AE009952_GR.
Gene locus YP_3281 in contig AE017042_GR.
Gene locus YPO3767 in contig AL590842_GR.
KEGGype:YPO3767.
ypk:y0463.
ypm:YP_3281.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG370930.
OMAAIDDIYW.

Enzyme and pathway databases

BioCycYPES187410:Y0463-MONOMER.
YPES214092:YPO3767-MONOMER.
YPES229193:YP3281-MONOMER.
BRENDA2.3.1.16. 142588.

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. 1 hit.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
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_YERPE
AccessionPrimary (citable) accession number: Q8ZAM9
Secondary accession number(s): Q0WAP2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2002
Last modified: February 9, 2010
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents