Reviewed, UniProtKB/Swiss-Prot Q15ZF4 (FADA_PSEA6)

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:	Patl_0202

Organism

Pseudoalteromonas atlantica (strain T6c / BAA-1087) [Complete proteome] [HAMAP]

Taxonomic identifier

342610 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Pseudoalteromonadaceae › Pseudoalteromonas

Protein attributes

Sequence length	386 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 – 386	386	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000292893
Sites
	Active site	91	1	Acyl-thioester intermediate By similarity
	Active site	342	1	Proton acceptor By similarity
	Active site	372	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q15ZF4-1 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: DF386109E53941B6	FASTA	386	40,796
	10 20 30 40 50 60 MKEVVVVDCI RTPMGRSKGG IFRNVRAETL SAHLMSKLIE RNPNLDPNEI EDIIWGCVQQ 70 80 90 100 110 120 TKEQGFNIAR NAQLLTDIPR SVAAVTVNRL CGSSMQALHD ATSGIMSGRG DVYMIGGVEH 130 140 150 160 170 180 MGHVPMDFNI DFHPGIAKTA ARASGSMGMT AELLGRQNGI SREMQDAFGA RSHQKAHAAA 190 200 210 220 230 240 VEGRWNEIVA TEGHDADGIL KLIDADETIR PDSTTESMSG LRPVFDPVNG TVTAGTSSAL 250 260 270 280 290 300 SDGASAMLIM SADKAKALGL TPRAKIRAMA VAGCDAAIMG FGPVPATQKA LKRAGMTMAD 310 320 330 340 350 360 IELAEFNEAF AAQALSCIKQ LGWLDTYEDK VNLNGGAIAL GHPLGCSGSR ISTTLINLME 370 380 ANDKSIGLAT MCIGLGQGIA TVFERV

References

[1]

"Complete sequence of Pseudoalteromonas atlantica T6c." 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., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000388 Genomic DNA. Translation: ABG38734.1.
RefSeq	YP_659788.1.
3D structure databases
SMR	Q15ZF4. Positions 2-386.
ModBase	Search...
Protein-protein interaction databases
STRING	Q15ZF4.
Genome annotation databases
GeneID	4171748.
GenomeReviews	Gene locus Patl_0202 in contig CP000388_GR.
KEGG	pat:Patl_0202.
NMPDR	fig|342610.3.peg.2221.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HBG370930.
OMA	AFGARSH.
PhylomeDB	Q15ZF4.
Enzyme and pathway databases
BioCyc	PATL342610:PATL_0202-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. 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_PSEA6

Accession

Primary (citable) accession number: Q15ZF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	July 25, 2006
Last modified:	February 9, 2010
This is version 31 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)