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Q7U1J9 (MMAA2_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. 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 MmaA2

Short name=CMAS
EC=2.1.1.79
Alternative name(s):
Cyclopropane-fatty-acyl-phospholipid synthase
Short name=CFA synthase
Mycolic acid methyltransferase
Short name=MA-MT
S-adenosylmethionine-dependent methyltransferase
Short name=AdoMet-MT
Short name=SAM-MT
Gene names
Name:cmaC
Synonyms:mmaA2, mmas-2
Ordered Locus Names:Mb0663c
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length287 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence By similarity. Ref.1

Catalytic activity

S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.

Pathway

Lipid metabolism; mycolic acid biosynthesis.

Sequence similarities

Belongs to the CFA/CMAS family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 287287Cyclopropane mycolic acid synthase MmaA2
PRO_0000398360

Regions

Region33 – 342S-adenosyl-L-methionine binding By similarity
Region72 – 743S-adenosyl-L-methionine binding By similarity
Region94 – 996S-adenosyl-L-methionine binding By similarity
Region123 – 1242S-adenosyl-L-methionine binding By similarity

Sites

Active site2691 By similarity
Binding site1361S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Experimental info

Sequence conflict2081I → S in AAC44874. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q7U1J9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 4894FF920B090129

FASTA28732,681
        10         20         30         40         50         60 
MVNDLTPHFE DVQAHYDLSD DFFRLFLDPT QTYSCAHFER EDMTLEEAQI AKIDLALGKL 

        70         80         90        100        110        120 
GLQPGMTLLD IGCGWGATMR RAIAQYDVNV VGLTLSKNQA AHVQKSFDEM DTPLDRRVLL 

       130        140        150        160        170        180 
AGWEQFNEPV DRIVSIGAFE HFGHDRHADF FARAHKILPP DGVLLLHTIT GLTRQQMVDH 

       190        200        210        220        230        240 
GLPLTLWLAR FLKFIATEIF PGGQPPTIEM VEEQSAKTGF TLTRRQSLQP HYARTLDLWA 

       250        260        270        280 
EALQEHKSEA IAIQSEEVYE RYMKYLTGCA KLFRVGYIDV NQFTLAK 

« Hide

References

« Hide 'large scale' references
[1]"Mycobacterium bovis BCG genes involved in the biosynthesis of cyclopropyl keto- and hydroxy-mycolic acids."
Dubnau E., Laneelle M.-A., Soares S., Benichou A., Vaz T., Prome D., Prome J.-C., Daffe M., Quemard A.
Mol. Microbiol. 23:313-322(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN OXYGEN-CONTAINING MYCOLATES BIOSYNTHESIS, NOMENCLATURE.
Strain: BCG / Pasteur.
[2]"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. expand/collapse author list , 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
U77466 Genomic DNA. Translation: AAC44874.1.
BX248333 Genomic DNA. Translation: CDO41907.1.
RefSeqNP_854321.1. NC_002945.3.

3D structure databases

ProteinModelPortalQ7U1J9.
SMRQ7U1J9. Positions 3-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb0663c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD93525; CAD93525; Mb0663c.
GeneID1091773.
KEGGmbo:Mb0663c.
PATRIC18003118. VBIMycBov88188_0723.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2230.
HOGENOMHOG000245191.
KOK00574.
OMAKDRQYSC.
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 nameMMAA2_MYCBO
AccessionPrimary (citable) accession number: Q7U1J9
Secondary accession number(s): P94923, X2BFN6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 67 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