B7N2F1 (B7N2F1_ECO81) 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 CAR10522.1
Ordered Locus Names:	ECED1_4547

Organism

Escherichia coli O81 (strain ED1a) [Complete proteome] [HAMAP]

Taxonomic identifier

585397 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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 SAAS SAAS012805 RuleBase RU003558 EMBL CAR10522.1 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)
	B7N2F1 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: A54868E8AC40C413	FASTA	387	40,805
	10 20 30 40 50 60 MEQVVIVDAI RTPMGRSKGG AFRNVRAEDL SAHLMRSLLA RNPALEAAAL DDIYWGCVQQ 70 80 90 100 110 120 TLEQGFNIAR NAALLAEVPH SVPAVTVNRL CGSSMQALHD AARMIMTGDA QACLVGGVEH 130 140 150 160 170 180 MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT AEMLARMHGI SREMQDAFAA RSHARAWAAT 190 200 210 220 230 240 QSGAFKNEII PTGGHDADGV LKQFNYDEVI RPETTVEALA TLRPAFDPVS GTVTAGTSSA 250 260 270 280 290 300 LSDGAAAMLV MSESRARELG LKPRARVRSM AVVGCDPSIM GYGPVPASKL ALKKAGLSAS 310 320 330 340 350 360 DIGVFEMNEA FAAQILPCIK DLGLIEQIDE KINLNGGAIA LGHPLGCSGA RISTTLLNLM 370 380 EHKDVQFGLA TMCIGLGQGI ATVFERV

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928162 Genomic DNA. Translation: CAR10522.1.
RefSeq	YP_002400349.1. NC_011745.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	B7N2F1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000142489; EBESCP00000136698; EBESCG00000144964.
GeneID	7142170.
GenomeReviews	Gene locus ECED1_4547 in contig CU928162_GR.
PATRIC	38493170. VBIEscCol8292_4536.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009707.
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.
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

B7N2F1_ECO81

Accession

Primary (citable) accession number: B7N2F1

Entry history

Integrated into UniProtKB/TrEMBL:	February 10, 2009
Last sequence update:	February 10, 2009
Last modified:	December 14, 2011
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)