Q99YD2 (FABH_STRP1) 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:	SPy_1754, M5005_Spy1494

Organism

Streptococcus pyogenes serotype M1 [Complete proteome] [HAMAP]

Taxonomic identifier

301447 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	324 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 – 324	324	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110493
Regions
	Region	250 – 254	5	ACP-binding By similarity
Sites
	Active site	112	1	By similarity
	Active site	249	1	By similarity
	Active site	279	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q99YD2 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: F27F9B82464E5903	FASTA	324	34,876
	10 20 30 40 50 60 MIFSKISQVA HYVPQQLVTN NDLASIMDTS HEWIFSRTGI AERHISRDEM TSDLAIQVAD 70 80 90 100 110 120 QLLTQSGLKA DAIDFIIVAT ISPDATMPST AAKVQAAIAA TSAFAFDMTA ACSGFVFALA 130 140 150 160 170 180 MADKLIASGA YQNGMVIGAE TLSKLVNWQD RATAVLFGDG AGGVLLEASK DKHVLAETLH 190 200 210 220 230 240 TDGARCQSLI SGETSLSSPY SIGKKAIATI QMDGRAIFDF AIRDVSKSIL TLMAQSDITK 250 260 270 280 290 300 DDIDYCLLHQ ANRRILDKIA RKIDVPREKF LENMMRYGNT SAASIPILLS EAVQKGQIRL 310 320 DGTQKILLSG FGGGLTWGSL IVRI

References

[1]	"Complete genome sequence of an M1 strain of Streptococcus pyogenes." Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K., Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L. , White J., Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E. Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001) [PubMed: 11296296] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700294 / SF370 / Serotype M1.
[2]	"Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events." Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M. J. Infect. Dis. 192:771-782(2005) [PubMed: 16088826] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-947 / MGAS5005 / Serotype M1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE004092 Genomic DNA. Translation: AAK34497.1. CP000017 Genomic DNA. Translation: AAZ52112.1.
RefSeq	NP_269776.1. NC_002737.1. YP_282857.1. NC_007297.1.
3D structure databases
ProteinModelPortal	Q99YD2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTRT00000000047; EBSTRP00000000047; EBSTRG00000000047. EBSTRT00000028402; EBSTRP00000027420; EBSTRG00000028402.
GeneID	3571417. 901989.
GenomeReviews	Gene locus SPy_1754 in contig AE004092_GR. Gene locus M5005_Spy1494 in contig CP000017_GR.
KEGG	spy:SPy_1754. spz:M5005_Spy_1494.
PATRIC	19716952. VBIStrPyo79812_1527.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000027516.
HOGENOM	HBG649927.
OMA	RGDCLNL.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	SPYO160490:SPY1754-MONOMER. SPYO293653:M5005_SPY1494-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_STRP1

Accession

Primary (citable) accession number: Q99YD2
Secondary accession number(s): Q48X13

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program