B5QW84 (B5QW84_SALEP) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended 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 EMBL CAR35352.1
Ordered Locus Names:	SEN3776

Organism

Salmonella enteritidis PT4 (strain P125109) [Complete proteome] [HAMAP]

Taxonomic identifier

550537 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella enteritidis

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Protein existence	Inferred 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 RuleBase RU003557

Ontologies

Keywords
Biological process	Fatty acid metabolism HAMAP MF_01620 SAAS SAAS020613 Lipid degradation HAMAP MF_01620 SAAS SAAS020613 Lipid metabolism
Cellular component	Cytoplasm HAMAP MF_01620 SAAS SAAS020613
Molecular function	Acyltransferase HAMAP MF_01620 RuleBase RU003558 SAAS SAAS012805 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: HAMAP lipid catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	91	1	Acyl-thioester intermediate By similarity HAMAP MF_01620
	Active site	343	1	Proton acceptor By similarity HAMAP MF_01620
	Active site	373	1	Proton acceptor By similarity HAMAP MF_01620

Sequences

	Sequence		Length	Mass (Da)
	B5QW84 [UniParc]. Last modified November 4, 2008. Version 1. Checksum: 9503B4E83617B40C	FASTA	387	40,977
	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 LKQFSYDEVI 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

References

[1]

"Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways." Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J. Genome Res. 18:1624-1637(2008) [PubMed: 18583645] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM933172 Genomic DNA. Translation: CAR35352.1.
RefSeq	YP_002245832.1. NC_011294.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	B5QW84.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6948343.
GenomeReviews	Gene locus SEN3776 in contig AM933172_GR.
KEGG	set:SEN3776.
PATRIC	32338248. VBISalEnt14964_3857.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG370930.
OMA	AIDDIYW.
ProtClustDB	PRK08947.
Family and domain databases
HAMAP	MF_01620. FadA. [Tree]
InterPro	IPR012805. 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]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.
KO	K00632.
PANTHER	PTHR18919:SF35. PTHR18919:SF35. 1 hit. PTHR18919. Thiolase. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAM	SSF53901. Thiolase-like. 2 hits.
TIGRFAMs	TIGR01930. AcCoA-C-Actrans. 1 hit. TIGR02445. FadA. 1 hit.
PROSITE	PS00098. THIOLASE_1. 1 hit. PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

B5QW84_SALEP

Accession

Primary (citable) accession number: B5QW84

Entry history

Integrated into UniProtKB/TrEMBL:	November 4, 2008
Last sequence update:	November 4, 2008
Last modified:	December 14, 2011
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)