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P0A2H7 (FADA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:STM3982
ORF Names:STMD1.7
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

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 term3D-structure
Complete proteome
Reference 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_0000206391

Sites

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

Secondary structure

1 ................................................ 387
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A2H7 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 39E24805360ABD8A

FASTA38741,004
        10         20         30         40         50         60 
MEQVVIVDAI RTPMGRSKGG AFRNVRAEDL SAHLMRSLLA RNPSLTAATL DDIYWGCVQQ 

        70         80         90        100        110        120 
TLEQGFNIAR NAALLAEIPH SVPAVTVNRL CGSSMQALHD AARMIMTGDA QVCLVGGVEH 

       130        140        150        160        170        180 
MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT AEMLSRLHGI SREMQDQFAA RSHARAWAAT 

       190        200        210        220        230        240 
QSGAFKTEII PTGGHDADGV LKQFNYDEVI RPETTVEALS TLRPAFDPVS GTVTAGTSSA 

       250        260        270        280        290        300 
LSDGAAAMLV MSESRARELG LKPRARIRSM AVVGCDPSIM GYGPVPASKL ALKKAGLSAS 

       310        320        330        340        350        360 
DIDVFEMNEA FAAQILPCIK DLGLMEQIDE KINLNGGAIA LGHPLGCSGA RISTTLINLM 

       370        380 
ERKDAQFGLA TMCIGLGQGI ATVFERV

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF233324 Genomic DNA. Translation: AAF33416.1.
AE006468 Genomic DNA. Translation: AAL22826.1.
RefSeqNP_462867.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GOAX-ray1.70A/B1-387[»]
ProteinModelPortalP0A2H7.
SMRP0A2H7. Positions 4-387.
ModBaseSearch...

Proteomic databases

PRIDEP0A2H7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1255508.
GenomeReviewsGene locus STM3982 in contig AE006468_GR.
KEGGstm:STM3982.
PATRIC32386832. VBISalEnt20916_4201.

Phylogenomic databases

HOGENOMHBG370930.
OMAAIDDIYW.
ProtClustDBPRK08947.

Enzyme and pathway databases

BioCycSTYP99287:STM3982-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 nameFADA_SALTY
AccessionPrimary (citable) accession number: P0A2H7
Secondary accession number(s): Q9L6L6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 25, 2012
This is version 49 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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