Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q49807 (CMAS2_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. 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
Ordered Locus Names:ML2426
ORF Names:B2168_F3_130
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length308 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 – 308308Cyclopropane mycolic acid synthase 2
PRO_0000089568

Regions

Region44 – 452S-adenosyl-L-methionine binding By similarity
Region79 – 879S-adenosyl-L-methionine binding By similarity
Region105 – 1106S-adenosyl-L-methionine binding By similarity
Region137 – 1382S-adenosyl-L-methionine binding By similarity

Sites

Active site2901 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q49807 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9068380ED6D324AA

FASTA30835,132
        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 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00018 Genomic DNA. Translation: AAA17222.1.
AL583925 Genomic DNA. Translation: CAC31942.1.
PIRS72886.
RefSeqNP_302570.1. NC_002677.1.

3D structure databases

ProteinModelPortalQ49807.
SMRQ49807. Positions 15-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML2426.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC31942; CAC31942; CAC31942.
GeneID908573.
KEGGmle:ML2426.
PATRIC18059499. VBIMycLep78757_4664.

Organism-specific databases

LepromaML2426.
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_MYCLE
AccessionPrimary (citable) accession number: Q49807
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 87 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