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Q79FX6 (MMAA2_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:mmaA2
Synonyms:mma2
Ordered Locus Names:Rv0644c
OrganismMycobacterium tuberculosis (strain ATCC 25618 / H37Rv) [Reference proteome] [HAMAP]
Taxonomic identifier83332 [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. Ref.2 Ref.6

Catalytic activity

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

Enzyme regulation

Inhibited by S-adenosyl-N-decyl-aminoethyl (SADAE) and thiacetazone (TAC). Ref.3 Ref.5

Pathway

Lipid metabolism; mycolic acid biosynthesis.

Disruption phenotype

Disruption of this gene suppresses a cyclopropane group at the distal position of alpha mycolic acid and cause a mild impairment in methoxymycolate, but not in ketomycolate. A 2-fold reduction in the relative abundance of cis-cyclopropanated methoxymycolate is observed. Cells lacking both cmA2 and mmaA2 genes cannot cis cyclopropanate methoxymycolates or ketomycolates. Ref.2

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_0000398359

Regions

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

Sites

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

Secondary structure

............................................. 287
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q79FX6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 669C3224C6B178C0

FASTA28732,724
        10         20         30         40         50         60 
MVNDLTPHFE DVQAHYDLSD DFFRLFLDPT QTYSCAHFER EDMTLEEAQI AKIDLALGKL 

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

       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]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"The mmaA2 gene of Mycobacterium tuberculosis encodes the distal cyclopropane synthase of the alpha-mycolic acid."
Glickman M.S.
J. Biol. Chem. 278:7844-7849(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE BIOSYNTHESIS OF CYCLOPROPANE RING IN THE ALPHA MYCOLATE, DISRUPTION PHENOTYPE.
Strain: ATCC 35801 / TMC 107 / Erdman.
[3]"Thiacetazone, an antitubercular drug that inhibits cyclopropanation of cell wall mycolic acids in mycobacteria."
Alahari A., Trivelli X., Guerardel Y., Dover L.G., Besra G.S., Sacchettini J.C., Reynolds R.C., Coxon G.D., Kremer L.
PLoS ONE 2:E1343-E1343(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
Strain: ATCC 25618 / H37Rv.
[4]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
[5]"S-adenosyl-N-decyl-aminoethyl, a potent bisubstrate inhibitor of mycobacterium tuberculosis mycolic acid methyltransferases."
Vaubourgeix J., Bardou F., Boissier F., Julien S., Constant P., Ploux O., Daffe M., Quemard A., Mourey L.
J. Biol. Chem. 284:19321-19330(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
Strain: ATCC 25618 / H37Rv.
[6]"Redundant function of cmaA2 and mmaA2 in Mycobacterium tuberculosis cis cyclopropanation of oxygenated mycolates."
Barkan D., Rao V., Sukenick G.D., Glickman M.S.
J. Bacteriol. 192:3661-3668(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN OXYGEN-CONTAINING MYCOLATES AND IN ALPHA-MYCOLATES BIOSYNTHESIS.
[7]"Structure of the cyclopropane synthase mmaA2 from Mycobacterium tuberculosis."
Smith C.V., Sacchettini J.C.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH S-ADENOSYLMETHIONINE.
Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL123456 Genomic DNA. Translation: CCP43387.1.
RefSeqNP_215158.1. NC_000962.3.
YP_006513985.1. NC_018143.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TPYX-ray2.20A1-287[»]
ProteinModelPortalQ79FX6.
SMRQ79FX6. Positions 3-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING83332.Rv0644c.

Proteomic databases

PRIDEQ79FX6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCP43387; CCP43387; Rv0644c.
GeneID13318530.
888061.
KEGGmtu:Rv0644c.
mtv:RVBD_0644c.
PATRIC18149942. VBIMycTub87468_0719.

Organism-specific databases

TubercuListRv0644c.

Phylogenomic databases

eggNOGCOG2230.
HOGENOMHOG000245191.
KOK00574.
OMAWKQADTL.
OrthoDBEOG6BGNZP.
ProtClustDBCLSK790562.

Enzyme and pathway databases

BioCycMetaCyc:RV0644C-MONOMER.
MTBRV:RV0644C-MONOMER.
UniPathwayUPA00915.

Family and domain databases

InterProIPR003333. Mycolic_cyclopropane_synthase.
[Graphical view]
PfamPF02353. CMAS. 1 hit.
[Graphical view]
PIRSFPIRSF003085. CMAS. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ79FX6.

Entry information

Entry nameMMAA2_MYCTU
AccessionPrimary (citable) accession number: Q79FX6
Secondary accession number(s): L0T7B6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 71 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways