Q9Z8P0 (FABH_CHLPN) 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:	CPn_0298, CP_0460, CpB0307

Organism

Chlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]

Taxonomic identifier

83558 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

Protein attributes

Sequence length	335 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	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. 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: InterPro 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_0000110414
Regions
	Region	262 – 266	5	ACP-binding By similarity
Sites
	Active site	120	1	By similarity
	Active site	261	1	By similarity
	Active site	291	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Z8P0 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 4895DE74DBE0DB60	FASTA	335	36,081
	10 20 30 40 50 60 MWFSVNKNKK AAIWATGSYL PEKVLSNADL EKMVDTSDEW IVTRTGIKER RIAGPQEYTS 70 80 90 100 110 120 LMGAIAAEKA IANAGLSKDQ IDCIIFSTAA PDYIFPSSGA LAQAHLGIED VPTFDCQAAC 130 140 150 160 170 180 TGYLYGLSVA KAYVESGTYN HVLLIAADKL SSFVDYTDRN TCVLFGDGGA ACVIGESRPG 190 200 210 220 230 240 SLEINRLSLG ADGKLGELLS LPAGGSRCPA SKETLQSGKH FIAMEGKEVF KHAVRRMETA 250 260 270 280 290 300 AKHSIALAGI QEEDIDWFVP HQANERIIDA LAKRFEIDES RVFKSVHKYG NTAASSVGIA 310 320 330 LDELVHTESI KLDDYLLLVA FGGGLSWGAV VLKQV

References

[1]	"Comparative genomes of Chlamydia pneumoniae and C. trachomatis." Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S. Nat. Genet. 21:385-389(1999) [PubMed: 10192388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CWL029.
[2]	"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M. Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AR39.
[3]	"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA." Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T. Nucleic Acids Res. 28:2311-2314(2000) [PubMed: 10871362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J138.
[4]	"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis." Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TW-183.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001363 Genomic DNA. Translation: AAD18447.1. AE002161 Genomic DNA. Translation: AAF38297.1. BA000008 Genomic DNA. Translation: BAA98508.1. AE009440 Genomic DNA. Translation: AAP98240.1.
PIR	B86528. F72096.
RefSeq	NP_224503.1. NC_000922.1. NP_300357.1. NC_002491.1. NP_445008.1. NC_002179.2. NP_876583.1. NC_005043.1.
3D structure databases
ProteinModelPortal	Q9Z8P0.
ModBase	Search...
2D gel databases
PHCI-2DPAGE	Q9Z8P0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1466990. 895109. 919081. 963748.
GenomeReviews	Gene locus CPn_0298 in contig AE001363_GR. Gene locus CP_0460 in contig AE002161_GR. Gene locus CpB0307 in contig AE009440_GR. Gene locus fabH in contig BA000008_GR.
KEGG	cpa:CP0460. cpn:CPn0298. cpt:CpB0307.
TIGR	CP_0460.
Phylogenomic databases
HOGENOM	HBG649927.
OMA	DAYIRGG.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	CPNE115711:CP_0460-MONOMER. CPNE115713:CPN0298-MONOMER. CPNE138677:CPJ0298-MONOMER. CPNE182082:CPB0307-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_CHLPN

Accession

Primary (citable) accession number: Q9Z8P0
Secondary accession number(s): Q9JQ91

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program