P0A5P1 (CMAS2_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclopropane mycolic acid synthase 2
Short name=CMAS
EC=2.1.1.79

Alternative name(s):
Cyclopropane-fatty-acyl-phospholipid synthase
Short name=CFA synthase
Short name=Cyclopropane fatty acid synthase
Mycolic acid methyltransferase
Short name=MA-MT
S-adenosylmethionine-dependent methyltransferase
Short name=AdoMet-MT
Short name=SAM-MT

Gene names

Name:	cmaA2
Synonyms:	cma2
Ordered Locus Names:	Mb0515c

Organism

Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]

Taxonomic identifier

233413 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence By similarity.
Catalytic activity	S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.
Pathway	Lipid metabolism; mycolic acid biosynthesis.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the CFA/CMAS family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	lipid biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cyclopropane-fatty-acyl-phospholipid 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 – 302	302	Cyclopropane mycolic acid synthase 2		PRO_0000089567
Regions
	Region	41 – 42	2	S-adenosyl-L-methionine binding By similarity
	Region	76 – 84	9	S-adenosyl-L-methionine binding By similarity
	Region	102 – 107	6	S-adenosyl-L-methionine binding By similarity
	Region	131 – 132	2	S-adenosyl-L-methionine binding By similarity
Sites
	Active site	284	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A5P1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 63AAA95627F95755	FASTA	302	34,660
	10 20 30 40 50 60 MTSQGDTTSG TQLKPPVEAV RSHYDKSNEF FKLWLDPSMT YSCAYFERPD MTLEEAQYAK 70 80 90 100 110 120 RKLALDKLNL EPGMTLLDIG CGWGSTMRHA VAEYDVNVIG LTLSENQYAH DKAMFDEVDS 130 140 150 160 170 180 PRRKEVRIQG WEEFDEPVDR IVSLGAFEHF ADGAGDAGFE RYDTFFKKFY NLTPDDGRML 190 200 210 220 230 240 LHTITIPDKE EAQELGLTSP MSLLRFIKFI LTEIFPGGRL PRISQVDYYS SNAGWKVERY 250 260 270 280 290 300 HRIGANYVPT LNAWADALQA HKDEAIALKG QETYDIYMHY LRGCSDLFRD KYTDVCQFTL VK

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248335 Genomic DNA. Translation: CAD93378.1.
RefSeq	NP_854178.1. NC_002945.3.
3D structure databases
ProteinModelPortal	P0A5P1.
SMR	P0A5P1. Positions 12-302.
ModBase	Search...
Protein-protein interaction databases
STRING	233413.Mb0515c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD93378; CAD93378; Mb0515c.
GeneID	1091574.
KEGG	mbo:Mb0515c.
PATRIC	18002785. VBIMycBov88188_0561.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2230.
HOGENOM	HOG000245191.
KO	K00574.
OMA	TLMAWHA.
ProtClustDB	CLSK790562.
Enzyme and pathway databases
UniPathway	UPA00915.
Family and domain databases
InterPro	IPR003333. Mycolic_cyclopropane_synthase. [Graphical view]
Pfam	PF02353. CMAS. 1 hit. [Graphical view]
PIRSF	PIRSF003085. CMAS. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CMAS2_MYCBO

Accession

Primary (citable) accession number: P0A5P1
Secondary accession number(s): Q11196

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program