A6QFJ3 (FABH_STAAE) 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:	NWMN_0853

Organism

Staphylococcus aureus (strain Newman) [Complete proteome] [HAMAP]

Taxonomic identifier

426430 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	313 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 – 313	313	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP-Rule MF_01815		PRO_1000073682
Regions
	Region	239 – 243	5	ACP-binding By similarity
Sites
	Active site	112	1	By similarity
	Active site	238	1	By similarity
	Active site	268	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6QFJ3 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 325F4A9CFF461769	FASTA	313	33,879
	10 20 30 40 50 60 MNVGIKGFGA YAPEKIIDNA YFEQFLDTSD EWISKMTGIK ERHWADDDQD TSDLAYEASL 70 80 90 100 110 120 KAIADAGIQP EDIDMIIVAT ATGDMPFPTV ANMLQERLGT GKVASMDQLA ACSGFMYSMI 130 140 150 160 170 180 TAKQYVQSGD YHNILVVGAD KLSKITDLTD RSTAVLFGDG AGAVIIGEVS DGRGIISYEM 190 200 210 220 230 240 GSDGTGGKHL YLDKDTGKLK MNGREVFKFA VRIMGDASTR VVEKANLTSD DIDLFIPHQA 250 260 270 280 290 300 NIRIMESARE RLGISKDKMS VSVNKYGNTS AASIPLSIDQ ELKNGKIKDD DTIVLVGFGG 310 GLTWGAMTIK WGK

References

[1]

"Genome sequence of Staphylococcus aureus strain Newman and comparative analysis of staphylococcal genomes: polymorphism and evolution of two major pathogenicity islands." Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K. J. Bacteriol. 190:300-310(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Newman.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP009351 Genomic DNA. Translation: BAF67125.1.
RefSeq	YP_001331887.1. NC_009641.1.
3D structure databases
ProteinModelPortal	A6QFJ3.
SMR	A6QFJ3. Positions 1-312.
ModBase	Search...
Protein-protein interaction databases
STRING	426430.NWMN_0853.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAF67125; BAF67125; NWMN_0853.
GeneID	5330502.
KEGG	sae:NWMN_0853.
PATRIC	19585195. VBIStaAur133992_0926.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HOG000246674.
KO	K00648.
OMA	GAINALC.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	SAUR426430:GIXC-854-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...
Other
BindingDB	A6QFJ3.

Entry information

Entry name

FABH_STAAE

Accession

Primary (citable) accession number: A6QFJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	August 21, 2007
Last modified:	May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program