Reviewed, UniProtKB/Swiss-Prot Q0C312 (FABH_HYPNA)

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:	HNE_1162

Organism

Hyphomonas neptunium (strain ATCC 15444) [Complete proteome] [HAMAP]

Taxonomic identifier

228405 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Hyphomonadaceae › Hyphomonas

Protein attributes

Sequence length	323 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 – 323	323	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000056368
Regions
	Region	251 – 255	5	ACP-binding By similarity
Sites
	Active site	114	1	By similarity
	Active site	250	1	By similarity
	Active site	280	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0C312-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 2C55285BB6B14A44	FASTA	323	34,173
	10 20 30 40 50 60 MGRRSFIRGT GSYLPERVLT NDELSEMVET TDAWIQERTG IKKRHVAADG ELTSDIAVHA 70 80 90 100 110 120 ARRALEAAGM QASEIDLIVL ATTTPDQTFP ATATAVQAKL GTGPGAAFDV QAVCSGFLFA 130 140 150 160 170 180 LATADSLMKQ GLFHKALVIG AETFTRIIDW SDRGTCVLFG DGGGAIVLEC VEWDGADDAG 190 200 210 220 230 240 VITHHVRTDG TKSNLLYVDG GVSSTGTIGH VRMEGNKVFK HAVTNISAAI EAVLTETGLT 250 260 270 280 290 300 SADIDWFVPH QANKRILDGV AKKMSIPEEK VVITVSEHAN TSAASIPLAL DHVVRSGRAK 310 320 PGDLILSEAM GGGFSWGASL FRL

References

[1]

"Comparative genomic evidence for a close relationship between the dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter crescentus." Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R., Brinkac L.M. , Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N., Ward N.L. J. Bacteriol. 188:6841-6850(2006) [PubMed: 16980487] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000158 Genomic DNA. Translation: ABI77101.1.
RefSeq	YP_759881.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0C312.
Genome annotation databases
GeneID	4289152.
GenomeReviews	Gene locus HNE_1162 in contig CP000158_GR.
KEGG	hne:HNE_1162.
NMPDR	fig|228405.5.peg.1131.
TIGR	HNE_1162.
Phylogenomic databases
HOGENOM	Q0C312.
OMA	ITRGAAF.
Enzyme and pathway databases
BioCyc	HNEP81032:HNE_1162-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_HYPNA

Accession

Primary (citable) accession number: Q0C312

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 17, 2006
Last modified:	November 3, 2009
This is version 27 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)