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A1S1I7 (FADA_SHEAM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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:Sama_0031
OrganismShewanella amazonensis (strain ATCC BAA-1098 / SB2B) [Complete proteome] [HAMAP]
Taxonomic identifier326297 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

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

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 – 3873873-ketoacyl-CoA thiolase HAMAP MF_01620
PRO_0000292900

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A1S1I7 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: BF03FB097B40DE1D

FASTA38740,635
        10         20         30         40         50         60 
MKQAVIVDCI RTPMGRSKGG VFRNVRAETL SAELMKALLL RNPGVDPNTI EDVIWGCVQQ 

        70         80         90        100        110        120 
TLEQGFNIAR NASLLAGVPK TAGAVTVNRL CGSSMEALHQ ASRAIMTGMG DTFIIGGVEH 

       130        140        150        160        170        180 
MGHVPMNHGV DFHPGLAANV AKASGMMGLT AEMLGKLHGI SREMQDQFAV RSHQRAHAAS 

       190        200        210        220        230        240 
IEGRFANEIY AIEGHDANGA LIKVDYDEVI RPETTLESLA GLRPVFDPAN GTVTAGTSSA 

       250        260        270        280        290        300 
LSDGAAAMLV MEEEKARALG LTIRARVRSM AVAGCDAAIM GYGPVPATQK ALARAGLSIQ 

       310        320        330        340        350        360 
DMDVIELNEA FAAQSLPCVK DLGLMDVVED KVNLNGGAIA LGHPLGCSGA RISTTLINLM 

       370        380 
EHKDATLGLA TMCIGLGQGI ATVFERV 

« Hide

References

[1]"Complete sequence of Shewanella amazonensis SB2B."
US DOE Joint Genome Institute
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1098 / SB2B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000507 Genomic DNA. Translation: ABL98243.1.
RefSeqYP_925913.1. NC_008700.1.

3D structure databases

ProteinModelPortalA1S1I7.
SMRA1S1I7. Positions 2-387.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1S1I7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4602288.
GenomeReviewsGene locus Sama_0031 in contig CP000507_GR.
KEGGsaz:Sama_0031.
NMPDRfig|326297.7.peg.27.
PATRIC23448533. VBISheAma74963_0030.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHBG370930.
OMASSMEAIH.
PhylomeDBA1S1I7.
ProtClustDBPRK08947.

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_SHEAM
AccessionPrimary (citable) accession number: A1S1I7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 39 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