Reviewed, UniProtKB/Swiss-Prot Q820E6 (FABH_CHLCV)

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:	CCA_00484

Organism

Chlamydophila caviae [Complete proteome] [HAMAP]

Taxonomic identifier

83557 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydophila

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier-protein] + CoA + CO2. HAMAP MF_01815
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Probable.
Domain	The last Arg residue of the ACP-binding site is essential for the weak association between ACP/acpP and fabH By similarity.
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: 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: HAMAP beta-ketoacyl-acyl-carrier-protein synthase III 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 – 335	335	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110412
Regions
	Region	260 – 264	5	ACP-binding By similarity
Sites
	Active site	118	1	By similarity
	Active site	259	1	By similarity
	Active site	289	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q820E6-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: E4C4ECD3E17903D0	FASTA	335	35,770
	10 20 30 40 50 60 MCVKKIRKAS IWATGSYLPE KILSNSDLEQ MVDTSDEWIV TRTGIKERRI AAPGEYASIM 70 80 90 100 110 120 GAKAAEKAIE KAGLTKDQIE CIIFSTSAPD YIFPSSAALA QAYLGIKEVP AFDCMAACTG 130 140 150 160 170 180 YLYGLSVAKA LVESGAYNNV LLIAADKLSS FVNYEDRNTC VLFGDGGSAC VVGESRPGAL 190 200 210 220 230 240 EITNVNLGAD GSVADLLSLP AGGSRLPASP ETVAEGKHFI YMEGKEVFKH AVRRMESAAK 250 260 270 280 290 300 ICIAEAGLAE GDIDWLVPHQ ANERIIDAIA KRFEIDESKV FKTLSKYGNT AASSVCIALD 310 320 330 ELLQLHVINS GEYLLLVAFG GGLSWGAVVL RQVEG

References

[1]

"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae." Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. , Rank R.G., Bavoil P.M., Fraser C.M. Nucleic Acids Res. 31:2134-2147(2003) [PubMed: 12682364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GPIC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE015925 Genomic DNA. Translation: AAP05228.1.
RefSeq	NP_829350.1.
3D structure databases
HSSP	HSSP built from PDB template 1HNK based on UniProtKB P24249.
ModBase	Search...
Genome annotation databases
GeneID	1218169.
GenomeReviews	Gene locus CCA_00484 in contig AE015925_GR.
KEGG	cca:CCA00484.
TIGR	CCA_00484.
Phylogenomic databases
HOGENOM	Q820E6.
OMA	WATGSYL.
Enzyme and pathway databases
BioCyc	CCAV227941:CCA_00484-MON.
BRENDA	2.3.1.180. 304519.
Family and domain databases
HAMAP	MF_01815. [Tree]
InterPro	IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
Pfam	PF08545. ACP_syn_III. 1 hit. PF08541. ACP_syn_III_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR00747. fabH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FABH_CHLCV

Accession

Primary (citable) accession number: Q820E6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 46 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)