Q49807 (CMAS2_MYCLE) 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
Ordered Locus Names:	ML2426
ORF Names:	B2168_F3_130

Organism

Mycobacterium leprae (strain TN) [Complete proteome] [HAMAP]

Taxonomic identifier

272631 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium leprae

Protein attributes

Sequence length	308 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 – 308	308	Cyclopropane mycolic acid synthase 2		PRO_0000089568
Regions
	Region	44 – 45	2	S-adenosyl-L-methionine binding By similarity
	Region	79 – 87	9	S-adenosyl-L-methionine binding By similarity
	Region	105 – 110	6	S-adenosyl-L-methionine binding By similarity
	Region	137 – 138	2	S-adenosyl-L-methionine binding By similarity
Sites
	Active site	290	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q49807 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 9068380ED6D324AA	FASTA	308	35,132
	10 20 30 40 50 60 MVPSQSHPAK TPRKQLKPPI EAVQSHYDRS NEFFKLWLDP SMTYSCAYFE RPDLTLEEAQ 70 80 90 100 110 120 RAKRDLALSK LGLEPGMTLL DIGCGWGSTM LHAIEKYDVN VIGLTLSANQ LAHNKLKFAE 130 140 150 160 170 180 IDHTRTDRTK DVRLQGWEQF DEPVDRIISL GAFEHFADGA GDAGFERYDS FFKMCYDVLP 190 200 210 220 230 240 DDGRMLLHTI IVPDAKETKE LGLTTPMSLL RFIKFILTEI FPGGRLPKIS QVDHYSSNAG 250 260 270 280 290 300 FTVERYHRIG SHYVPTLNAW AAALEAHKDE AIALQGRQIY DTYMHYLTGC SDLFRDRYTD VCQFTLVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Smith D.R., Robison K. Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00018 Genomic DNA. Translation: AAA17222.1. AL583925 Genomic DNA. Translation: CAC31942.1.
PIR	S72886.
RefSeq	NP_302570.1. NC_002677.1.
3D structure databases
ProteinModelPortal	Q49807.
SMR	Q49807. Positions 15-308.
ModBase	Search...
Protein-protein interaction databases
STRING	272631.ML2426.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC31942; CAC31942; CAC31942.
GeneID	908573.
KEGG	mle:ML2426.
PATRIC	18059499. VBIMycLep78757_4664.
Organism-specific databases
Leproma	ML2426.
CMR	Search...
Phylogenomic databases
eggNOG	COG2230.
HOGENOM	HOG000245191.
KO	K00574.
OMA	DASWERY.
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_MYCLE

Accession

Primary (citable) accession number: Q49807

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program