Q7MZ91 (FADA_PHOLL) 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:	plu4403

Organism

Photorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP]

Taxonomic identifier

243265 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus

Protein attributes

Sequence length	388 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 – 388	388	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000206377
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)
	Q7MZ91 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: C5076CBEBDAB0086	FASTA	388	41,382
	10 20 30 40 50 60 MENVVIIDGI RTPMGRSKGG AFRQVRAEDL SAHLMKKLFK RNPAIQQHEI DDIYWGCVQQ 70 80 90 100 110 120 TLEQGFNIAR NAALLADIPH SVPAVTVNRL CGSSMQALHD GARMIMTGEA NVTLIGGVEH 130 140 150 160 170 180 MGHVPMTHGV DFHPKMSLSV AKAAGVMGLT AEMLAKIHHI SREMQDEFAL RSHQRATQAT 190 200 210 220 230 240 QSGAFANEIS PIYGHDADGI LKRFDYDEVI RSDANLKDLA ALRPVFDPVT GSVTAGSSSA 250 260 270 280 290 300 LSDGASAMLI TSESYAKNLG LKPRARIRSM AAVGCDPSIM GYGPVPATQM ALKKAGLVLG 310 320 330 340 350 360 DIGVIELNEA FAAQSLACLK GLNLLDSMDD KVNLNGGAIA LGHPLGCSGA RITTTLLNLM 370 380 ERRDVQFGLA TMCIGLGQGI ATIIERMD

References

[1]

"The genome sequence of the entomopathogenic bacterium Photorhabdus luminescens." Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., Lanois A., Powell K. , Siguier P., Vincent R., Wingate V., Zouine M., Glaser P., Boemare N., Danchin A., Kunst F. Nat. Biotechnol. 21:1307-1313(2003) [PubMed: 14528314] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TT01.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571873 Genomic DNA. Translation: CAE16775.1.
RefSeq	NP_931576.1. NC_005126.1.
3D structure databases
ProteinModelPortal	Q7MZ91.
SMR	Q7MZ91. Positions 3-387.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2804424.
GenomeReviews	Gene locus plu4403 in contig BX470251_GR.
KEGG	plu:plu4403.
NMPDR	fig|243265.1.peg.4199.
PATRIC	20513512. VBIPhoLum48522_4992.
Organism-specific databases
GenoList	plu4403.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG370930.
OMA	QDIVNIN.
PhylomeDB	Q7MZ91.
ProtClustDB	PRK08947.
Enzyme and pathway databases
BioCyc	PLUM243265:PLU4403-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_PHOLL

Accession

Primary (citable) accession number: Q7MZ91

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 15, 2003
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program