A0PLS8 (FABH_MYCUA) Reviewed, UniProtKB/Swiss-Prot

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:	MUL_0632

Organism

Mycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]

Taxonomic identifier

362242 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
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. HAMAP MF_01815
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. HAMAP MF_01815
Subcellular location	Cytoplasm Probable HAMAP MF_01815.
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
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: 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_1000056380
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)
	A0PLS8 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: EB9E449AE4C3DAEF	FASTA	335	34,807
	10 20 30 40 50 60 MTEIATTSGI SSVGLLSVGA YRPTRVVTND EICENIDSSD EWIYSRTGIK TRRFAAPEES 70 80 90 100 110 120 AASMAIEASR EAIAKAALTG SDIDGVIVAT STHFLQTPAC APIVAAALGC QNVPAFDISA 130 140 150 160 170 180 GCSGFGHALG IAADMIRGGS AATILVIGTE KLSPTVDMTD RSNCFIFVDG AASVLVGHSP 190 200 210 220 230 240 IQGIGPTVWG SDGEQAAAIR QDIDWISHAE NPAGPRPFLR MEGTAVFRWA AFEMGKVGQQ 250 260 270 280 290 300 AMDAAGVKPD EIDVFIPHQA NSRINELLTK NLQLRPDAVI ANDIEHTGNT SAASIPLAMA 310 320 330 ELLATGAAKP GDLALLIGYG AGLSYAAQVV RMPNS

References

[1]

"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer." Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T. Genome Res. 17:192-200(2007) [PubMed: 17210928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Agy99.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000325 Genomic DNA. Translation: ABL03297.1.
RefSeq	YP_904768.1. NC_008611.1.
3D structure databases
ProteinModelPortal	A0PLS8.
SMR	A0PLS8. Positions 1-333.
ModBase	Search...
Protein-protein interaction databases
STRING	A0PLS8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000074554; EBMYCP00000072559; EBMYCG00000074549.
GeneID	4551629.
GenomeReviews	Gene locus MUL_0632 in contig CP000325_GR.
KEGG	mul:MUL_0632.
PATRIC	18167879. VBIMycUlc37413_0807.
Organism-specific databases
GenoList	MUL_0632.
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
GeneTree	EBGT00050000016069.
HOGENOM	HBG649927.
OMA	TIWGSDG.
ProtClustDB	PRK09352.
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	K11608.
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

FABH_MYCUA

Accession

Primary (citable) accession number: A0PLS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 9, 2007
Last modified:	December 14, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program