Reviewed, UniProtKB/Swiss-Prot Q3IJ24 (FADA_PSEHT)

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:	PSHAa0010

Organism

Pseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]

Taxonomic identifier

326442 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Pseudoalteromonadaceae › Pseudoalteromonas

Protein attributes

Sequence length	389 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 – 389	389	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000292894
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)
	Q3IJ24-1 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 2BAD62B06E15D50A	FASTA	389	40,918
	10 20 30 40 50 60 MNNPVIVDCI RTPMGRSKGG VFKNKRAEDL SAHLMKGLLD RNPAVDPASI DDIYWGCVQQ 70 80 90 100 110 120 TLEQGFNVAR NAALLAGIPH SVPAVTVNRL CGSSMQALHD AARAIMTGAG DTYLIGGVEH 130 140 150 160 170 180 MGHVPMTHGN DFHPGLATSI AQAAGSMGLT AEYLATLHGI SREQQDEFAY RSHQRAQAAT 190 200 210 220 230 240 VEGRFRREIL AMEGHAADGS LILVEDDEVI RPETTVEGLS KLRPVFNPAS GTVTAGTSSA 250 260 270 280 290 300 LSDGASAMLV MSEAKAKELG LPIRARIKAM AVAGCDPSIM GYGPVPASKK ALAQAGITID 310 320 330 340 350 360 DLGVVELNEA FAAQSLPVMK DLGLMDVVDE KVNLNGGAIA LGHPLGCSGS RISTSLIHLM 370 380 EDKNVRYGLA TMCIGLGQGI ATVFERVQD

References

[1]

"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125." Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A. Genome Res. 15:1325-1335(2005) [PubMed: 16169927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR954246 Genomic DNA. Translation: CAI85124.1.
RefSeq	YP_338567.1.
3D structure databases
HSSP	HSSP built from PDB template 2D3T based on UniProtKB P28790.
SMR	Q3IJ24. Positions 5-387.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3IJ24.
Genome annotation databases
GeneID	3709118.
GenomeReviews	Gene locus PSHAa0010 in contig CR954246_GR.
KEGG	pha:PSHAa0010.
NMPDR	fig|326442.4.peg.21.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HBG370930.
OMA	SSMEAIH.
PhylomeDB	Q3IJ24.
Enzyme and pathway databases
BioCyc	PHAL326442:PSHAA0010-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_PSEHT

Accession

Primary (citable) accession number: Q3IJ24

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	November 8, 2005
Last modified:	February 9, 2010
This is version 36 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)