Reviewed, UniProtKB/Swiss-Prot Q0BTE0 (FABH_GRABC)

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:	GbCGDNIH1_1014

Organism

Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1) [Complete proteome] [HAMAP]

Taxonomic identifier

391165 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Granulibacter

Protein attributes

Sequence length	322 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: 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 322	322	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000070231
Regions
	Region	250 – 254	5	ACP-binding By similarity
Sites
	Active site	113	1	By similarity
	Active site	249	1	By similarity
	Active site	279	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0BTE0-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 55B83DB4614F3B28	FASTA	322	33,962
	10 20 30 40 50 60 MKRSIIAGVG AYLPSTVVSN DELAKRVDTS DAWIRERTGI EQRYLATADE SCAFMAARAA 70 80 90 100 110 120 ERALAHAGMT ADDVDAILVA TSTPDQVFPA VAVRVQALLG AKRGFGFDLS AACSGFVYGL 130 140 150 160 170 180 SMGDALIRSG QAKGVLVIGA EVFSRLLDWD DRRTNVLFGD GAGAAFLRAS TDNDDPARGI 190 200 210 220 230 240 LSTHLHSEGE FGDILFIDGA NGVAGHPGTI VMNGREVFRH AVGKMAQAVE EAMAANDLTP 250 260 270 280 290 300 ADIDWLVPHQ ANLRIIEAMG KKLDLPPEKV VVTVNRHANT SAASIPLALN EAVQDGRIQP 310 320 GSVVLMEALG GGLTWGSAIL RM

References

[1]

"Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis." Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M. J. Bacteriol. 189:8727-8736(2007) [PubMed: 17827295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000394 Genomic DNA. Translation: ABI61912.1.
RefSeq	YP_744835.1.
3D structure databases
SMR	Q0BTE0. Positions 4-321.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0BTE0.
Genome annotation databases
GeneID	4275838.
GenomeReviews	Gene locus GbCGDNIH1_1014 in contig CP000394_GR.
KEGG	gbe:GbCGDNIH1_1014.
NMPDR	fig|391165.8.peg.1016.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	ITERRFA.
PhylomeDB	Q0BTE0.
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.
Pfam	PF08545. ACP_syn_III. 1 hit. PF08541. ACP_syn_III_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR00747. fabH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FABH_GRABC

Accession

Primary (citable) accession number: Q0BTE0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 17, 2006
Last modified:	February 9, 2010
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)