Reviewed, UniProtKB/Swiss-Prot Q0I0T4 (FADA_SHESR)

Names and origin

Protein names

Recommended name:
    3-ketoacyl-CoA thiolase
    EC=2.3.1.16
Alternative name(s):
    Fatty acid oxidation complex subunit beta
    Beta-ketothiolase
    Acetyl-CoA acyltransferase

Gene names

Name:	fadA
Ordered Locus Names:	Shewmr7_0015

Organism

Shewanella sp. (strain MR-7) [Complete proteome] [HAMAP]

Taxonomic identifier

60481 [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
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. HAMAP MF_01620
Subcellular location	Cytoplasm By similarity HAMAP MF_01620.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
Cellular component	Cytoplasm
Molecular function	Acyltransferase 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
Molecule processing
	Chain	1 – 387	387	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000292906
Sites
	Active site	91	1	Acyl-thioester intermediate By similarity
	Active site	343	1	Proton acceptor By similarity
	Active site	373	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0I0T4-1 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: 62B3D39A40ABE7FB	FASTA	387	40,623
	10 20 30 40 50 60 MKQAVIVDCI RTPMGRSKAG VFRNVRAETL SAELMKGLLL RNPQLDPNAI EDVIWGCVQQ 70 80 90 100 110 120 TLEQGFNIAR NASLLAGIPK TAGAVTVNRL CGSSMEAIHQ AARAIMTGMG DTFIIGGVEH 130 140 150 160 170 180 MGHVPMNHGV DFHPGLANNV AKASGMMGLT AEMLGKLHGI SREQQDAFAV RSHQRAHAAT 190 200 210 220 230 240 VEGRFAKEIY AIEGHDANGA LIKVLHDEVI RPETSMESLA ALRPVFDPAN GTVTAGTSSA 250 260 270 280 290 300 LSDGASAMLV MEESKARALG LPIRARIRSM AVAGCDAAIM GYGPVPATQK ALARAGITVN 310 320 330 340 350 360 DLDVIELNEA FAAQSLPCVK DLGLLDVVDE KINLNGGAIA LGHPLGCSGA RISTTLINLM 370 380 EHKDATLGLA TMCIGLGQGI ATVFERV

References

[1]

"Complete sequence of chromosome 1 of Shewanella sp. MR-7." 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., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., Tiedje J., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000444 Genomic DNA. Translation: ABI41021.1.
RefSeq	YP_736078.1.
3D structure databases
SMR	Q0I0T4. Positions 2-387.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0I0T4.
Genome annotation databases
GeneID	4258048.
GenomeReviews	Gene locus Shewmr7_0015 in contig CP000444_GR.
KEGG	shm:Shewmr7_0015.
NMPDR	fig|60481.10.peg.15.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HBG370930.
OMA	SSMEAIH.
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. 1 hit.
PANTHER	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.
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

FADA_SHESR

Accession

Primary (citable) accession number: Q0I0T4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	October 3, 2006
Last modified:	February 9, 2010
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)