Q5QXH8 (FADA_IDILO) 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:	IL0010

Organism

Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]

Taxonomic identifier

283942 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina

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.
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 – 387	387	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000206375
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)
	Q5QXH8 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 602455AADFD7FAA9	FASTA	387	41,249
	10 20 30 40 50 60 MKDIVIVDCI RTPMGRSKNG VFRHTRAEDL SAALMKGLLE RNPEVDPEEL EDIYWGCVQQ 70 80 90 100 110 120 TLEQGFNIAR NSALIAGIPH KVAGVTVNRL CGSSMQALHD ATRAIMNGDG DIFMAGGVEH 130 140 150 160 170 180 MGHVPMTHGI DFHPGMNKSV AKASGSMGMT AELLSRKFGI TREQQDEFGA RSHRKAHEAT 190 200 210 220 230 240 VEGRFAKEIY AMNGHNADGE LVRVTEDEVI RPETTAEGLS QLRPVFDPAN GTVTAGTSSA 250 260 270 280 290 300 LSDGAAAMLV MSADKAKELG LTPRVKIRSM AVAGCDPSIM GYGPVPATEK ALKRAGVSID 310 320 330 340 350 360 DIDVVELNEA FAAQSLPVLK GLKLFDKMEE KVNLNGGAIA LGHPLGCSGA RISTTLINLM 370 380 EEKDAKLGLA TMCIGLGQGI ATVFERV

References

[1]

"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy." Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. , Aizawa S., Shibata S., Malahoff A., Alam M. Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017340 Genomic DNA. Translation: AAV80854.1.
RefSeq	YP_154403.1. NC_006512.1.
3D structure databases
ProteinModelPortal	Q5QXH8.
SMR	Q5QXH8. Positions 2-387.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3174456.
GenomeReviews	Gene locus IL0010 in contig AE017340_GR.
KEGG	ilo:IL0010.
NMPDR	fig|283942.3.peg.60.
PATRIC	22138025. VBIIdiLoi21852_0010.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG370930.
OMA	QDIVNIN.
ProtClustDB	PRK08947.
Enzyme and pathway databases
BioCyc	ILOI283942:IL0010-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_IDILO

Accession

Primary (citable) accession number: Q5QXH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program