Reviewed, UniProtKB/Swiss-Prot Q1IQ32 (FABH_ACIBL)

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:	Acid345_2017

Organism

Acidobacteria bacterium (strain Ellin345) [Complete proteome] [HAMAP]

Taxonomic identifier

204669 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Candidatus Koribacter

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Subcellular location	Cytoplasm Probable.
Domain	The last Arg residue of the ACP-binding site is essential for the weak association between ACP/acpP and fabH By similarity.
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 – 333	333	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000070210
Regions
	Region	259 – 263	5	ACP-binding By similarity
Sites
	Active site	116	1	By similarity
	Active site	258	1	By similarity
	Active site	288	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1IQ32-1 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: 4CB8727FF8DAAA2D	FASTA	333	35,995
	10 20 30 40 50 60 MTSVRRAKIT ALGTYVPPRV LSNFDLEKMV DTTNQWILER TGIRERHLVD KGVAASDLAV 70 80 90 100 110 120 EAAKKCLANR GIEAAEVECI VVGTVTPDMM YPSTACLVQH KLGIPNAWGF DVSAGCSGFL 130 140 150 160 170 180 FSLTTGAKFI ESGQYKKVLV IGSDVNSSMI DYTDRATCII FGDGAGAVLL EPTEDGEDVG 190 200 210 220 230 240 VMDHIHQVEG VGGQYLYMPG GGSLNPASHE TIDQKMHYVH QDGQNVFKYA VKKMSEMTEK 250 260 270 280 290 300 VLKRNSLTGT DVDCFIAHQA NKRIIVATAE RLKMPMEKVI INIEKYGNTT AGTIPLAMQT 310 320 330 ALDEGKLKKG SNVLLAAVGA GFTSGATLLR WAF

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000360 Genomic DNA. Translation: ABF41018.1.
RefSeq	YP_591092.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1IQ32.
Genome annotation databases
GeneID	4070347.
GenomeReviews	Gene locus Acid345_2017 in contig CP000360_GR.
KEGG	aba:Acid345_2017.
NMPDR	fig|204669.6.peg.2004.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1IQ32.
OMA	FKSAVTS.
Family and domain databases
HAMAP	MF_01815. [Tree]
InterPro	IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. 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_ACIBL

Accession

Primary (citable) accession number: Q1IQ32

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	June 13, 2006
Last modified:	November 3, 2009
This is version 26 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)