Q3B6K8 (FABH_PELLD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3
EC=2.3.1.41

Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III
Beta-ketoacyl-ACP synthase III
Short name=KAS III

Gene names

Name:	fabH
Ordered Locus Names:	Plut_0133

Organism

Pelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM 273)) [Complete proteome] [HAMAP]

Taxonomic identifier

319225 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Pelodictyon

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids By similarity. HAMAP MF_01815
Catalytic activity	Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. HAMAP MF_01815
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815
Subunit structure	Homodimer By similarity. HAMAP MF_01815
Subcellular location	Cytoplasm Probable HAMAP MF_01815.
Domain	The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP MF_01815
Sequence similarities	Belongs to the FabH family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-oxoacyl-[acyl-carrier-protein] synthase 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 – 329	329	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000056387
Regions
	Region	256 – 260	5	ACP-binding By similarity
Sites
	Active site	113	1	By similarity
	Active site	255	1	By similarity
	Active site	285	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3B6K8 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: FF4D0D3443073657	FASTA	329	35,591
	10 20 30 40 50 60 MNAAISATAR YLPEGVLSNL DLERMLDTND EWIRSRTGIS ERRILRDPKK ATSYMCGEVA 70 80 90 100 110 120 SQLLRKRGLA AEELELIIVA TMTPDMMFPS TACLVQDIIG AKNAWAFDIN AACSGFLYAL 130 140 150 160 170 180 NTASQFIKAG THKNVMVIGG DKMSSIIDYT DRSTAILFGD GAGGVILEAA ESEGFGVLDA 190 200 210 220 230 240 RMYSDGTNGK DHLLMKGGGS LHPATHDTVD QHLHYIYQDG RMVFKSAVTS MADVAAEIME 250 260 270 280 290 300 RNGLTSDDVS WLVPHQANQR IISATAERMG IDESKVISNV GRYGNTTAGT IPICLSELDD 310 320 GGHLEHGSNL VLVSFGAGYT WGGVYVKWQ

References

[1]

"Complete sequence of Pelodictyon luteolum DSM 273." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 273.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000096 Genomic DNA. Translation: ABB23023.1.
RefSeq	YP_374066.1. NC_007512.1.
3D structure databases
ProteinModelPortal	Q3B6K8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3B6K8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3744690.
GenomeReviews	Gene locus Plut_0133 in contig CP000096_GR.
KEGG	plt:Plut_0133.
NMPDR	fig|319225.3.peg.276.
PATRIC	21377699. VBIChlLut1287_0139.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	QANTRIV.
PhylomeDB	Q3B6K8.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	PLUT319225:PLUT_0133-MONOMER.
Family and domain databases
HAMAP	MF_01815. FabH. [Tree]
InterPro	IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
KO	K00648.
Pfam	PF08545. ACP_syn_III. 1 hit. PF08541. ACP_syn_III_C. 1 hit. [Graphical view]
SUPFAM	SSF53901. Thiolase-like. 1 hit.
TIGRFAMs	TIGR00747. FabH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FABH_PELLD

Accession

Primary (citable) accession number: Q3B6K8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 22, 2005
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program