A9KU90 (A9KU90_SHEB9) 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
Ordered Locus Names:	Sbal195_0019

Organism

Shewanella baltica (strain OS195) [Complete proteome] [HAMAP] EMBL ABX47201.1

Taxonomic identifier

399599 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

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

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 EMBL ABX47201.1 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)
	A9KU90 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: D8BE5A3984D9C175	FASTA	387	40,576
	10 20 30 40 50 60 MKQAVIVDCI RTPMGRSKAG VFRNVRAETL SAELMKGLLL RNPQLDPNLI EDVIWGCVQQ 70 80 90 100 110 120 TLEQGFNIAR NASLLAGIPK TAGAVTVNRL CGSSMDAIHQ AARAIMTGMG DTFIIGGVEH 130 140 150 160 170 180 MGHVPMSHGV DFHPGLANNV AKASGMMGLT AEMLGKLHGI TREQQDAFAV RSHQRAYAAT 190 200 210 220 230 240 VEGRFAKEIY GIEGHDANGA LIKVLQDEVI RPETTMESLA ALRPVFDPVN GTVTAGTSSA 250 260 270 280 290 300 LSDGASAMLI MEESKARALG LPIRARIRSM AVAGCDAAIM GYGPVPATQK ALARAGITVA 310 320 330 340 350 360 DLDVIELNEA FAAQSLPCVK DLGLADVVDD KINLNGGAIA LGHPLGCSGA RISTTLINLM 370 380 EDKDATLGLA TMCIGLGQGI ATVFERV

References

[1]

"Complete sequence of chromosome of Shewanella baltica OS195." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. , Brettar I., Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J., Richardson P. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OS195.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000891 Genomic DNA. Translation: ABX47201.1.
RefSeq	YP_001552461.1. NC_009997.1.
3D structure databases
ProteinModelPortal	A9KU90.
SMR	A9KU90. Positions 2-387.
ModBase	Search...
Protein-protein interaction databases
STRING	A9KU90.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5751711.
GenomeReviews	Gene locus Sbal195_0019 in contig CP000891_GR.
KEGG	sbn:Sbal195_0019.
PATRIC	23465934. VBISheBal33754_0020.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG370930.
OMA	SSMEAIH.
ProtClustDB	PRK08947.
Enzyme and pathway databases
BioCyc	SBAL399599:SBAL195_0019-MONOMER.
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

A9KU90_SHEB9

Accession

Primary (citable) accession number: A9KU90

Entry history

Integrated into UniProtKB/TrEMBL:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)