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A8FP62 (A8FP62_SHESH) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-ketoacyl-CoA thiolase HAMAP MF_01620
EC=2.3.1.16 HAMAP MF_01620
Alternative name(s):
Acetyl-CoA acyltransferase HAMAP MF_01620
Beta-ketothiolase HAMAP MF_01620
Fatty acid oxidation complex subunit beta HAMAP MF_01620
Gene names
Name:fadA HAMAP MF_01620
Ordered Locus Names:Ssed_0022
OrganismShewanella sediminis (strain HAW-EB3) [Complete proteome] [HAMAP] EMBL ABV34635.1
Taxonomic identifier425104 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

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 By similarity. HAMAP MF_01620

Catalytic activity

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. HAMAP MF_01620 SAAS SAAS020613

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01620 SAAS SAAS020613

Subunit structure

Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity. HAMAP MF_01620 SAAS SAAS020613

Subcellular location

Cytoplasm By similarity HAMAP MF_01620.

Sequence similarities

Belongs to the thiolase family. HAMAP MF_01620

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site911Acyl-thioester intermediate By similarity HAMAP MF_01620
Active site3431Proton acceptor By similarity HAMAP MF_01620
Active site3731Proton acceptor By similarity HAMAP MF_01620

Sequences

Sequence LengthMass (Da)Tools
A8FP62 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 204BAD74FF496800

FASTA38740,943
        10         20         30         40         50         60 
MKQAVIVDCI RTPMGRSKAG VFRNVRAETL SAELMKALLV RNPQLDPNTI EDVIWGCVQQ 

        70         80         90        100        110        120 
TLEQGFNIAR NASLLAGLPK QIGGVTVNRL CGSSMDALHQ AARAIMTGQG DTFIIGGVEH 

       130        140        150        160        170        180 
MGHVPMNHGV DFHPGLANNV AKASGMMGLT AEMLGKMHGI TREQQDEFAV RSHQRAHAAT 

       190        200        210        220        230        240 
VEGRFANEIH PIEGHDADGA LIKVEHDEVI RPETSMESLS GLRPAFDPAN GTVTAGTSSA 

       250        260        270        280        290        300 
LSDGASAMLV MEEEKAKALG LPIRARIRSM AVAGCDAAIM GYGPVPATKK ALERANLSID 

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

       370        380 
EAKDAKYGLA TMCIGLGQGI ATIFERP

« Hide

References

[1]"Complete sequence of Shewanella sediminis HAW-EB3."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Zhao J.-S., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAW-EB3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000821 Genomic DNA. Translation: ABV34635.1.
RefSeqYP_001471763.1. NC_009831.1.

3D structure databases

ProteinModelPortalA8FP62.
SMRA8FP62. Positions 2-386.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8FP62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5612854.
GenomeReviewsGene locus Ssed_0022 in contig CP000821_GR.
KEGGsse:Ssed_0022.
NMPDRfig|425104.3.peg.19.
PATRIC23557170. VBISheSed62411_0023.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHBG370930.
OMASSMEAIH.
ProtClustDBPRK08947.

Enzyme and pathway databases

BioCycSSED425104:SSED_0022-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 nameA8FP62_SHESH
AccessionPrimary (citable) accession number: A8FP62
Entry history
Integrated into UniProtKB/TrEMBL: November 13, 2007
Last sequence update: November 13, 2007
Last modified: December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info