O07600 (FABH2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2
EC=2.3.1.180

Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III protein 2
Beta-ketoacyl-ACP synthase III 2
Short name=KAS III 2
bFabH2

Gene names

Name:	fabHB
Synonyms:	fabH2, yhfB
Ordered Locus Names:	BSU10170

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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. Has some substrate specificity for branched chain acyl-CoA, determining the biosynthesis of branched-chain of fatty acids instead of straight-chain. Ref.3
Catalytic activity	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. 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.
Induction	Down-regulated by FapR. Ref.4
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 Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: InterPro 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 – 325	325	3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2 HAMAP MF_01815		PRO_0000110400
Regions
	Region	251 – 255	5	ACP-binding By similarity
Sites
	Active site	113	1	By similarity
	Active site	250	1	By similarity
	Active site	280	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O07600 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: CE6E475F3C88E335	FASTA	325	35,424
	10 20 30 40 50 60 MSKAKITAIG TYAPSRRLTN ADLEKIVDTS DEWIVQRTGM RERRIADEHQ FTSDLCIEAV 70 80 90 100 110 120 KNLKSRYKGT LDDVDMILVA TTTSDYAFPS TACRVQEYFG WESTGALDIN ATCAGLTYGL 130 140 150 160 170 180 HLANGLITSG LHQKILVIAG ETLSKVTDYT DRTTCVLFGD AAGALLVERD EETPGFLASV 190 200 210 220 230 240 QGTSGNGGDI LYRAGLRNEI NGVQLVGSGK MVQNGREVYK WAARTVPGEF ERLLHKAGLS 250 260 270 280 290 300 SDDLDWFVPH SANLRMIESI CEKTPFPIEK TLTSVEHYGN TSSVSIVLAL DLAVKAGKLK 310 320 KDQIVLLFGF GGGLTYTGLL IKWGM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene." Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S. Microbiology 144:859-875(1998) [PubMed: 9579061] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis." Choi K.-H., Heath R.J., Rock C.O. J. Bacteriol. 182:365-370(2000) [PubMed: 10629181] [Abstract] Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
[4]	"FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis." Schujman G.E., Paoletti L., Grossman A.D., de Mendoza D. Dev. Cell 4:663-672(2003) [PubMed: 12737802] [Abstract] Cited for: INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y14083 Genomic DNA. Translation: CAA74523.1. AL009126 Genomic DNA. Translation: CAB12857.1.
PIR	H69829.
RefSeq	NP_388898.1. NC_000964.3.
3D structure databases
ProteinModelPortal	O07600.
SMR	O07600. Positions 4-324.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000002452; EBBACP00000002452; EBBACG00000002447.
GeneID	939306.
GenomeReviews	Gene locus BSU10170 in contig AL009126_GR.
KEGG	bsu:BSU10170.
NMPDR	fig|224308.1.peg.1017.
PATRIC	18973732. VBIBacSub10457_1060.
Organism-specific databases
GenoList	BSU10170. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000001269.
HOGENOM	HBG649927.
OMA	AIENLCT.
PhylomeDB	O07600.
ProtClustDB	PRK12879.
Enzyme and pathway databases
BioCyc	BSUB:BSU10170-MONOMER.
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.
KO	K00648.
Pfam	PF08545. ACP_syn_III. 1 hit. PF08541. ACP_syn_III_C. 1 hit. [Graphical view]
SUPFAM	SSF53901. Thiolase-like. 1 hit.
TIGRFAMs	TIGR00747. FabH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FABH2_BACSU

Accession

Primary (citable) accession number: O07600

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program