Q9KQH9 (FABF_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 2
EC=2.3.1.179

Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase II
Beta-ketoacyl-ACP synthase II
Short name=KAS II

Gene names

Name:	fabF
Ordered Locus Names:	VC_2019

Organism

Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]

Taxonomic identifier

243277 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › Vibrio cholerae › Vibrio cholerae O1 › Vibrio cholerae O1 biovar El Tor

Protein attributes

Sequence length	414 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis By similarity.
Catalytic activity	(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the beta-ketoacyl-ACP synthases family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from sequence or structural similarity Ref.1. Source: TIGR
Molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from sequence or structural similarity Ref.1. Source: TIGR beta-ketoacyl-acyl-carrier-protein synthase II 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 414	413	3-oxoacyl-[acyl-carrier-protein] synthase 2		PRO_0000180327
Sites
	Active site	164	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KQH9 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: EB5942D01274ED1F	FASTA	414	43,208
	10 20 30 40 50 60 MSKRRVVVTG MGMLSPVGNT VESSWKALLA GQSGIVNIEH FDTTNFSTRF AGLVKGFDCE 70 80 90 100 110 120 QYMSKKDARK MDLFIQYGIA AGIQALEDSG LEVNEENAAR IGVAIGSGIG GLELIETGHQ 130 140 150 160 170 180 ALIEKGPRKV SPFFVPSTIV NMIAGNLSIM RGLRGPNIAI STACTTGLHN IGHAARMIAY 190 200 210 220 230 240 GDADAMVAGG AEKASTPLGM AGFGAAKALS TRNDEPQKAS RPWDKDRDGF VLGDGAGIMV 250 260 270 280 290 300 LEEYEHAKAR GAKIYAEVVG FGMSGDAYHM TSPSEDGSGG ALAMEAAMRD AGVTGEQIGY 310 320 330 340 350 360 VNAHGTSTPA GDVAEVKGIK RALGEAGTKQ VLVSSTKSMT GHLLGAAGSV EAIITVMSLV 370 380 390 400 410 DQMVPPTINL DNPEEGLGVD LVPHVARKVE SMEYAMCNSF GFGGTNGSLI FKRM

References

[1]

"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003852 Genomic DNA. Translation: AAF95167.1.
PIR	D82128.
RefSeq	NP_231653.1. NC_002505.1.
3D structure databases
ProteinModelPortal	Q9KQH9.
SMR	Q9KQH9. Positions 3-414.
ModBase	Search...
Protein-protein interaction databases
STRING	243277.VC2019.
Proteomic databases
PRIDE	Q9KQH9.
Protocols and materials databases
DNASU	2613398.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF95167; AAF95167; VC_2019.
GeneID	2613398.
KEGG	vch:VC2019.
PATRIC	20083070. VBIVibCho83274_1929.
Phylogenomic databases
eggNOG	COG0304.
KO	K09458.
OMA	INMISGF.
ProtClustDB	PRK08722.
Enzyme and pathway databases
UniPathway	UPA00094.
Family and domain databases
Gene3D	3.40.47.10. 2 hits.
InterPro	IPR017568. 3-oxoacyl-ACP_synth-2. IPR018201. Ketoacyl_synth_AS. IPR014031. Ketoacyl_synth_C. IPR014030. Ketoacyl_synth_N. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view]
Pfam	PF00109. ketoacyl-synt. 1 hit. PF02801. Ketoacyl-synt_C. 1 hit. [Graphical view]
PIRSF	PIRSF000447. KAS_II. 1 hit.
SUPFAM	SSF53901. Thiolase-like. 2 hits.
TIGRFAMs	TIGR03150. fabF. 1 hit.
PROSITE	PS00606. B_KETOACYL_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FABF_VIBCH

Accession

Primary (citable) accession number: Q9KQH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program