Q4FQC7 (FADA_PSYA2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-ketoacyl-CoA thiolase
EC=2.3.1.16

Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Fatty acid oxidation complex subunit beta

Gene names

Name:	fadA
Ordered Locus Names:	Psyc_1933

Organism

Psychrobacter arcticus (strain DSM 17307 / 273-4) [Complete proteome] [HAMAP]

Taxonomic identifier

259536 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Psychrobacter

Protein attributes

Sequence length	390 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.
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: UniProtKB-KW lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 390	390	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000206387
Sites
	Active site	95	1	Acyl-thioester intermediate By similarity
	Active site	346	1	Proton acceptor By similarity
	Active site	376	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4FQC7 [UniParc]. Last modified August 30, 2005. Version 1. Checksum: 90911DC161B5FCA0	FASTA	390	41,395
	10 20 30 40 50 60 MTILSPKDVV IVDGVRSAMG KTKNGMFRHV RADSMSAELV RALVERNDFD PRDVEDIIWG 70 80 90 100 110 120 CVNQTLEQGL NIGRNIGLLA GIPKTAGGQT VNRLCGSSMQ ALHTAAAQIM TGQGDVFIIG 130 140 150 160 170 180 GVEHMGHVGM MHGIDLNPEA SKHYAKASNM MGLTAEMLGR MNNITREEQD AFGLESHRRA 190 200 210 220 230 240 WAATTEGRFD NEIIGIEGHD AAGRLQLCTV DEVIRPDATM EQMQKLRPAF DPVSGTVTAA 250 260 270 280 290 300 TSSALSDGAS AMLIMSAQKA KELGLKPRAR IRSMAVAGCD AAIMGYGPVP ATQKALKRAG 310 320 330 340 350 360 MSIEDMQTIE LNEAFAAQGL SVLKALNLTD KQDIVNINGG AIALGHPLGC SGARITVTLL 370 380 390 NAMEQSDTEI GLATMCIGLG QGISTIIERV

References

[1]

"The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth." Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M. Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed: 20154119] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 17307 / 273-4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000082 Genomic DNA. Translation: AAZ19781.1.
RefSeq	YP_265215.1. NC_007204.1.
3D structure databases
ProteinModelPortal	Q4FQC7.
SMR	Q4FQC7. Positions 4-390.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4FQC7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3515903.
GenomeReviews	Gene locus Psyc_1933 in contig CP000082_GR.
KEGG	par:Psyc_1933.
NMPDR	fig|259536.4.peg.1753.
PATRIC	23058761. VBIPsyArc98534_2285.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HBG370930.
OMA	QDIVNIN.
PhylomeDB	Q4FQC7.
ProtClustDB	PRK08947.
Enzyme and pathway databases
BioCyc	PARC259536:PSYC_1933-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

FADA_PSYA2

Accession

Primary (citable) accession number: Q4FQC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	August 30, 2005
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program