Reviewed, UniProtKB/Swiss-Prot P0A575 (FABH_MYCBO)

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:	Mb0547c

Organism

Mycobacterium bovis [Complete proteome] [HAMAP]

Taxonomic identifier

1765 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	335 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. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall 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 – 335	335	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110444
Regions
	Region	259 – 263	5	ACP-binding By similarity
Sites
	Active site	122	1	By similarity
	Active site	258	1	By similarity
	Active site	289	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A575-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 6573BE1FAE5BCFB6	FASTA	335	34,873
	10 20 30 40 50 60 MTEIATTSGA RSVGLLSVGA YRPERVVTND EICQHIDSSD EWIYTRTGIK TRRFAADDES 70 80 90 100 110 120 AASMATEACR RALSNAGLSA ADIDGVIVTT NTHFLQTPPA APMVAASLGA KGILGFDLSA 130 140 150 160 170 180 GCAGFGYALG AAADMIRGGG AATMLVVGTE KLSPTIDMYD RGNCFIFADG AAAVVVGETP 190 200 210 220 230 240 FQGIGPTVAG SDGEQADAIR QDIDWITFAQ NPSGPRPFVR LEGPAVFRWA AFKMGDVGRR 250 260 270 280 290 300 AMDAAGVRPD QIDVFVPHQA NSRINELLVK NLQLRPDAVV ANDIEHTGNT SAASIPLAMA 310 320 330 ELLTTGAAKP GDLALLIGYG AGLSYAAQVV RMPKG

References

[1]

"The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX248335 Genomic DNA. Translation: CAD93409.1.
RefSeq	NP_854208.1.
3D structure databases
SMR	P0A575. Positions 1-334.
ModBase	Search...
Genome annotation databases
GeneID	1091619.
GenomeReviews	Gene locus Mb0547c in contig BX248333_GR.
KEGG	mbo:Mb0547c.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A575.
OMA	TIWGSDG.
Enzyme and pathway databases
BRENDA	2.3.1.180. 3091.
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_MYCBO

Accession

Primary (citable) accession number: P0A575
Secondary accession number(s): O06399

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	November 3, 2009
This is version 32 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)