Reviewed, UniProtKB/Swiss-Prot Q606L3 (FABH_METCA)

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:	MCA2003

Organism

Methylococcus capsulatus [Complete proteome] [HAMAP]

Taxonomic identifier

414 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Methylococcales › Methylococcaceae › Methylococcus

Protein attributes

Sequence length	321 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	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier-protein] + CoA + CO2. 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 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 – 321	321	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000088314
Regions
	Region	249 – 253	5	ACP-binding By similarity
Sites
	Active site	114	1	By similarity
	Active site	248	1	By similarity
	Active site	278	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q606L3-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 97329C43DCCCE532	FASTA	321	34,697
	10 20 30 40 50 60 MSRYSRIAGT GGYLPRQVVT NDDLAMRVET SDEWIVERTG IRRRHIAAAD ETASSMAEIA 70 80 90 100 110 120 SRQALEAAAI DPHDLDLIIL ATSSPDRVFP STACLLQQRL GVRSCAAFDV QAACSGFIFA 130 140 150 160 170 180 LSIADQYISA GNANRVLVVG TEVNSRSVDW DDRSTCILFG DGAGAVVLES ATEPGIMSTH 190 200 210 220 230 240 IHSDGHYQDL LYLPNPASNG EGSDESRTIR MQGSEVFKVA VNTLGRIVDE TLEQNGLQKS 250 260 270 280 290 300 DVDWLVPHQA NIRIIAATAK KLQLPMERVV VTVDEQGNTS SASIPLAFDE AVRDGRIKRG 310 320 QTVLMEAFGG GFAWGSALLR Y

References

[1]

"Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath)." Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J. , Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A. PLoS Biol. 2:1616-1628(2004) [PubMed: 15383840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bath / NCIMB 11132.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017282 Genomic DNA. Translation: AAU91776.1.
RefSeq	YP_114435.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3103003.
GenomeReviews	Gene locus MCA2003 in contig AE017282_GR.
KEGG	mca:MCA2003.
NMPDR	fig|243233.4.peg.1954.
TIGR	MCA2003.
Phylogenomic databases
HOGENOM	Q606L3.
OMA	CEAYEEG.
Enzyme and pathway databases
BioCyc	MCAP243233:MCA_2003-MON.
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_METCA

Accession

Primary (citable) accession number: Q606L3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	November 23, 2004
Last modified:	November 3, 2009
This is version 37 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)