A4WTT9 (FABH_RHOS5) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3
EC=2.3.1.41

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:	Rsph17025_1912

Organism

Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) [Complete proteome] [HAMAP]

Taxonomic identifier

349102 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	323 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	Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. 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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 323	323	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000056397
Regions
	Region	251 – 255	5	ACP-binding By similarity
Sites
	Active site	114	1	By similarity
	Active site	250	1	By similarity
	Active site	280	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4WTT9 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: CE7E543EEA6D4613	FASTA	323	34,074
	10 20 30 40 50 60 MTIRAVVRGV GHYLPDRIVP NSELEALVET TDEWIRTRSG IERRHFAAEG QTTSDLAARA 70 80 90 100 110 120 ARAALADAGL QPDDIDTLIV ATSTADLTFP SAATMVQAAL GMSRGFAFDV QAVCAGFVYA 130 140 150 160 170 180 LANADALIRS GQANRVLVIG AETFSRLMDW SDRATCVLFG DGAGALVLEG AEGAGTSADR 190 200 210 220 230 240 GILATDLHSD GRFKDLLYVD GGASTGSTGH LRMQGREVFR HAVEKLAETA HTALDKAGLT 250 260 270 280 290 300 SADVDWIVPH QANLRIISAT AQRMQVPMDR VILTVQDHGN TSAASIPLAL SVGKARGQIK 310 320 EGDLLVTEAI GGGLAWGSVV LRW

References

[1]

"Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S. Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17025 / ATH 2.4.3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000661 Genomic DNA. Translation: ABP70803.1.
RefSeq	YP_001168108.1. NC_009428.1.
3D structure databases
ProteinModelPortal	A4WTT9.
ModBase	Search...
Protein-protein interaction databases
STRING	A4WTT9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5084037.
GenomeReviews	Gene locus Rsph17025_1912 in contig CP000661_GR.
KEGG	rsq:Rsph17025_1912.
PATRIC	23162116. VBIRhoSph94549_1977.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	TSDEWIW.
PhylomeDB	A4WTT9.
ProtClustDB	CLSK933877.
Enzyme and pathway databases
BioCyc	RSPH349102:RSPH17025_1912-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_RHOS5

Accession

Primary (citable) accession number: A4WTT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 29, 2007
Last modified:	January 25, 2012
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program