Q3KMC3 (FABH_CHLTA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3
EC=2.3.1.180

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:	CTA_0261

Organism

Chlamydia trachomatis serovar A (strain HAR-13 / ATCC VR-571B) [Complete proteome] [HAMAP]

Taxonomic identifier

315277 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Chlamydiae/Verrucomicrobia group › Chlamydiae › Chlamydiia › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia › Chlamydia trachomatis

Protein attributes

Sequence length	327 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-Rule MF_01815
Catalytic activity	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP-Rule MF_01815
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP-Rule MF_01815
Sequence similarities	Belongs to the FabH family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
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: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: InterPro beta-ketoacyl-acyl-carrier-protein synthase III 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 – 327	327	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP-Rule MF_01815		PRO_1000056341
Regions
	Region	254 – 258	5	ACP-binding By similarity
Sites
	Active site	112	1	By similarity
	Active site	253	1	By similarity
	Active site	283	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3KMC3 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 6D92252184B44A38	FASTA	327	35,327
	10 20 30 40 50 60 MRASIWGTGS YLPKKILTNA DLEKIVETSD EWISTRTGIK ERRIASAEEF SSFMGAKAAE 70 80 90 100 110 120 KAIEAAKISK SQVDCIVFST AAPDYIFPSS AALAQAYLGI KEIPAFDCLA ACTGFLYGLS 130 140 150 160 170 180 IAKAYVESGM YQCVLVIAAD KLSSFVNYQD RNTCVLFGDG GSACIVGHSR PGALEISKVN 190 200 210 220 230 240 LGADGKQGDL LRLPAGGSRC PASQDTVQNH QHFITMEGKE VFKHAVRRME FAAKTCITEA 250 260 270 280 290 300 GLQEKDIDWL VPHQANERII DAIAKRFAVK DSRVFKTLAK YGNTAASSVG IALDELLRTH 310 320 DIHVAERLLL VAFGGGLSWG AVILQQV

References

[1]

"Comparative genomic analysis of Chlamydia trachomatis oculotropic and genitotropic strains." Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D. Infect. Immun. 73:6407-6418(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HAR-13 / ATCC VR-571B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000051 Genomic DNA. Translation: AAX50499.1.
RefSeq	YP_328047.1. NC_007429.1.
3D structure databases
ProteinModelPortal	Q3KMC3.
ModBase	Search...
Protein-protein interaction databases
STRING	315277.CTA_0261.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAX50499; AAX50499; CTA_0261.
GeneID	3687415.
KEGG	cta:CTA_0261.
PATRIC	32022396. VBIChlTra31516_0268.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HOG000246674.
KO	K00648.
OMA	IHHGAAF.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	CTRA315277:GI4C-299-MONOMER.
UniPathway	UPA00094.
Family and domain databases
Gene3D	3.40.47.10. 2 hits.
HAMAP	MF_01815. FabH.
InterPro	IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view]
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_CHLTA

Accession

Primary (citable) accession number: Q3KMC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program