Q8EDH1 (FABH_SHEON) 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:	SO_2778

Organism

Shewanella oneidensis

Taxonomic identifier

70863 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length	319 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 Reference proteome
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 – 319	319	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110466
Regions
	Region	247 – 251	5	ACP-binding By similarity
Sites
	Active site	112	1	By similarity
	Active site	246	1	By similarity
	Active site	276	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8EDH1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 16D6D351B2B1DAF9	FASTA	319	34,026
	10 20 30 40 50 60 MHTKILGTGS YVPVQVRSNQ DLEKMVETSD QWIVERTGIS ERRIAAQDET VSTMGYLAAL 70 80 90 100 110 120 NALEMAGIEA SDLDMIICGT TSAANAFPAA ACEIQAMLGV HTIPAFDIAA ACSGFVYALS 130 140 150 160 170 180 VADQFVKNGT AKKVLVIGAD VLSRLCEPED RTTIILFGDG AGAAIIGASD EPGIISTHIY 190 200 210 220 230 240 ADGRQGDLLK CAFPPRQGET SEAVGFMTMK GNDVFKVAVT QLSHVVTETL RLNNIDKSEI 250 260 270 280 290 300 DWLVPHQANF RIINATAKKL DMSLDKVVLT LAKHGNTSAA SVPIALDEAV RDGRIQRGQL 310 LLLEAFGAGF AWGSALVRF

References

[1]

"Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis." Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., DeBoy R.T. , Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C., Nealson K.H., Fraser C.M. Nat. Biotechnol. 20:1118-1123(2002) [PubMed: 12368813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MR-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014299 Genomic DNA. Translation: AAN55803.1.
RefSeq	NP_718359.1. NC_004347.1.
3D structure databases
ProteinModelPortal	Q8EDH1.
SMR	Q8EDH1. Positions 1-319.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1170478.
GenomeReviews	Gene locus SO_2778 in contig AE014299_GR.
KEGG	son:SO_2778.
NMPDR	fig|211586.1.peg.2527.
PATRIC	23525191. VBISheOne101494_2678.
TIGR	SO_2778.
Phylogenomic databases
HOGENOM	HBG649927.
OMA	RILNFLA.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	SONE211586:SO_2778-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_SHEON

Accession

Primary (citable) accession number: Q8EDH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program