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Reviewed, UniProtKB/Swiss-Prot A4Y1B5 (FADA_SHEPC)

Last modified November 3, 2009. Version 22. 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: Sputcn32_0012
OrganismShewanella putrefaciens (strain CN-32 / ATCC BAA-453) [Complete proteome] [HAMAP]
Taxonomic identifier319224 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length387 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 – 3873873-ketoacyl-CoA thiolase HAMAP MF_01620
PRO_0000323555

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A4Y1B5-1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: D8BE5A3984D9C175

FASTA38740,576
        10         20         30         40         50         60 
MKQAVIVDCI RTPMGRSKAG VFRNVRAETL SAELMKGLLL RNPQLDPNLI EDVIWGCVQQ 

        70         80         90        100        110        120 
TLEQGFNIAR NASLLAGIPK TAGAVTVNRL CGSSMDAIHQ AARAIMTGMG DTFIIGGVEH 

       130        140        150        160        170        180 
MGHVPMSHGV DFHPGLANNV AKASGMMGLT AEMLGKLHGI TREQQDAFAV RSHQRAYAAT 

       190        200        210        220        230        240 
VEGRFAKEIY GIEGHDANGA LIKVLQDEVI RPETTMESLA ALRPVFDPVN GTVTAGTSSA 

       250        260        270        280        290        300 
LSDGASAMLI MEESKARALG LPIRARIRSM AVAGCDAAIM GYGPVPATQK ALARAGITVA 

       310        320        330        340        350        360 
DLDVIELNEA FAAQSLPCVK DLGLADVVDD KINLNGGAIA LGHPLGCSGA RISTTLINLM 

       370        380 
EDKDATLGLA TMCIGLGQGI ATVFERV 

« Hide

References

[1]"Complete sequence of Shewanella putrefaciens CN-32."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J., Tiedje J., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000681 Genomic DNA. Translation: ABP73748.1.
RefSeqYP_001181547.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA4Y1B5.

Genome annotation databases

GeneID5081487.
GenomeReviewsGene locus Sputcn32_0012 in contig CP000681_GR.
KEGGspc:Sputcn32_0012.
NMPDRfig|319224.13.peg.12.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMASSMEAIH.

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_SHEPC
AccessionPrimary (citable) accession number: A4Y1B5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 29, 2007
Last modified: November 3, 2009
This is version 22 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