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P0A5P1 (CMAS2_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Protein existenceInferred 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 processLipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlipid biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncyclopropane-fatty-acyl-phospholipid synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Cyclopropane mycolic acid synthase 2
PRO_0000089567

Regions

Region41 – 422S-adenosyl-L-methionine binding By similarity
Region76 – 849S-adenosyl-L-methionine binding By similarity
Region102 – 1076S-adenosyl-L-methionine binding By similarity
Region131 – 1322S-adenosyl-L-methionine binding By similarity

Sites

Active site2841 By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A5P1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 63AAA95627F95755

FASTA30234,660
        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 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248333 Genomic DNA. Translation: CDO41756.1.
RefSeqNP_854178.1. NC_002945.3.

3D structure databases

ProteinModelPortalP0A5P1.
SMRP0A5P1. Positions 12-302.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb0515c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD93378; CAD93378; Mb0515c.
GeneID1091574.
KEGGmbo:Mb0515c.
PATRIC18002785. VBIMycBov88188_0561.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2230.
HOGENOMHOG000245191.
KOK00574.
OMADASWERY.
OrthoDBEOG6BGNZP.

Enzyme and pathway databases

UniPathwayUPA00915.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR003333. Mycolic_cyclopropane_synthase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF02353. CMAS. 1 hit.
[Graphical view]
PIRSFPIRSF003085. CMAS. 1 hit.
SUPFAMSSF53335. SSF53335. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCMAS2_MYCBO
AccessionPrimary (citable) accession number: P0A5P1
Secondary accession number(s): Q11196, X2BFA2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: June 11, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways