Q82M29 (FABH2_STRAW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2
EC=2.3.1.180

Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III protein 2
Beta-ketoacyl-ACP synthase III 2
Short name=KAS III 2

Gene names

Name:	fabH2
Ordered Locus Names:	SAV_1831

Organism

Streptomyces avermitilis [Complete proteome] [HAMAP]

Taxonomic identifier

33903 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	315 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 – 315	315	3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2 HAMAP MF_01815		PRO_0000110482
Regions
	Region	242 – 246	5	ACP-binding By similarity
Sites
	Active site	113	1	By similarity
	Active site	241	1	By similarity
	Active site	271	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q82M29 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: E490D12CBA86583C	FASTA	315	32,372
	10 20 30 40 50 60 MNGSRIAAVG HYQPAKVLTN EDLASLVDTS DEWIRSRVGI RTRHFAGPDE PVDELAGHAA 70 80 90 100 110 120 AKALASAGLA PADIDLVLVA TSTAEDRSPN MAARVAARLG IPSPAAMDIN VVCAGFTHAL 130 140 150 160 170 180 ATADHAVRAG AATRALVIGA DKMSAVTDWS DRTTCVLVGD GAGAAVVDAC PEGAEPGIGP 190 200 210 220 230 240 VLWGSVPEMG HAVRIEGTPP RFAQEGQSVY RWATTQLPAI ARRACERAGL TPADLAGVVL 250 260 270 280 290 300 HQANLRIIEP LAAKIGAVNA VVARDVVESG NTSAASIPLA FSKLVERGEI STGDPVLLFG 310 FGGNLSYAGQ VIRCP

References

[1]

"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

[2]

"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis." Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S. Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000030 Genomic DNA. Translation: BAC69542.1.
RefSeq	NP_823007.1. NC_003155.4.
3D structure databases
ProteinModelPortal	Q82M29.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1210291.
GenomeReviews	Gene locus SAV_1831 in contig BA000030_GR.
KEGG	sma:SAV_1831.
NMPDR	fig|227882.1.peg.1833.
PATRIC	23717077. VBIStrAve112782_1952.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG649927.
OMA	SAYDINA.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	SAVE227882:SAV1831-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

FABH2_STRAW

Accession

Primary (citable) accession number: Q82M29

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program