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Reviewed, UniProtKB/Swiss-Prot Q15ZF4 (FADA_PSEA6)

Last modified November 3, 2009. Version 27. 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: Patl_0202
OrganismPseudoalteromonas atlantica (strain T6c / BAA-1087) [Complete proteome] [HAMAP]
Taxonomic identifier342610 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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 – 3863863-ketoacyl-CoA thiolase HAMAP MF_01620
PRO_0000292893

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q15ZF4-1 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: DF386109E53941B6

FASTA38640,796
        10         20         30         40         50         60 
MKEVVVVDCI RTPMGRSKGG IFRNVRAETL SAHLMSKLIE RNPNLDPNEI EDIIWGCVQQ 

        70         80         90        100        110        120 
TKEQGFNIAR NAQLLTDIPR SVAAVTVNRL CGSSMQALHD ATSGIMSGRG DVYMIGGVEH 

       130        140        150        160        170        180 
MGHVPMDFNI DFHPGIAKTA ARASGSMGMT AELLGRQNGI SREMQDAFGA RSHQKAHAAA 

       190        200        210        220        230        240 
VEGRWNEIVA TEGHDADGIL KLIDADETIR PDSTTESMSG LRPVFDPVNG TVTAGTSSAL 

       250        260        270        280        290        300 
SDGASAMLIM SADKAKALGL TPRAKIRAMA VAGCDAAIMG FGPVPATQKA LKRAGMTMAD 

       310        320        330        340        350        360 
IELAEFNEAF AAQALSCIKQ LGWLDTYEDK VNLNGGAIAL GHPLGCSGSR ISTTLINLME 

       370        380 
ANDKSIGLAT MCIGLGQGIA TVFERV 

« Hide

References

[1]"Complete sequence of Pseudoalteromonas atlantica T6c."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000388 Genomic DNA. Translation: ABG38734.1.
RefSeqYP_659788.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ15ZF4.

Genome annotation databases

GeneID4171748.
GenomeReviewsGene locus Patl_0202 in contig CP000388_GR.
KEGGpat:Patl_0202.
NMPDRfig|342610.3.peg.2221.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ15ZF4.
OMAAFGARSH.

Enzyme and pathway databases

BioCycPATL342610:PATL_0202-MON.

Family and domain databases

HAMAPMF_01620.
[Tree]
InterProIPR012805. FadA.
IPR002155. Thiolase.
IPR016038. Thiolase-like_subgr.
[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_PSEA6
AccessionPrimary (citable) accession number: Q15ZF4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: July 25, 2006
Last modified: November 3, 2009
This is version 27 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