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Q79FX6

- MMAA2_MYCTU

UniProt

Q79FX6 - MMAA2_MYCTU

Protein

Cyclopropane mycolic acid synthase MmaA2

Gene

mmaA2

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by S-adenosyl-N-decyl-aminoethyl (SADAE) and thiacetazone (TAC).2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei136 – 1361S-adenosyl-L-methionine; via carbonyl oxygen
    Active sitei269 – 2691By similarity

    GO - Molecular functioni

    1. cyclopropane-fatty-acyl-phospholipid synthase activity Source: UniProtKB
    2. methyltransferase activity Source: UniProtKB
    3. protein binding Source: MTBBASE

    GO - Biological processi

    1. mycolic acid biosynthetic process Source: MTBBASE

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:RV0644C-MONOMER.
    MTBRV:RV0644C-MONOMER.
    UniPathwayiUPA00915.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclopropane mycolic acid synthase MmaA2 (EC:2.1.1.79)
    Short name:
    CMAS
    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 namesi
    Name:mmaA2
    Synonyms:mma2
    Ordered Locus Names:Rv0644c
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001584: Chromosome

    Organism-specific databases

    TubercuListiRv0644c.

    Subcellular locationi

    GO - Cellular componenti

    1. cell wall Source: MTBBASE
    2. plasma membrane Source: MTBBASE

    Pathology & Biotechi

    Disruption phenotypei

    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.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 287286Cyclopropane mycolic acid synthase MmaA2PRO_0000398359Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylvaline1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ79FX6.

    Interactioni

    Protein-protein interaction databases

    STRINGi83332.Rv0644c.

    Structurei

    Secondary structure

    1
    287
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 168
    Helixi20 – 245
    Helixi45 – 5713
    Turni58 – 614
    Beta strandi67 – 726
    Helixi77 – 8610
    Beta strandi89 – 957
    Helixi97 – 10812
    Beta strandi116 – 1216
    Helixi123 – 1253
    Beta strandi131 – 1377
    Helixi139 – 1424
    Helixi144 – 1463
    Helixi147 – 15711
    Beta strandi163 – 1719
    Helixi174 – 1796
    Helixi186 – 19813
    Helixi208 – 21811
    Beta strandi221 – 2277
    Helixi229 – 24517
    Helixi247 – 2537
    Helixi256 – 27520
    Beta strandi277 – 28610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TPYX-ray2.20A1-287[»]
    ProteinModelPortaliQ79FX6.
    SMRiQ79FX6. Positions 3-287.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ79FX6.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni33 – 342S-adenosyl-L-methionine binding
    Regioni72 – 743S-adenosyl-L-methionine binding
    Regioni94 – 996S-adenosyl-L-methionine binding
    Regioni123 – 1242S-adenosyl-L-methionine binding

    Sequence similaritiesi

    Belongs to the CFA/CMAS family.Curated

    Phylogenomic databases

    eggNOGiCOG2230.
    HOGENOMiHOG000245191.
    KOiK00574.
    OMAiKDRQYSC.
    OrthoDBiEOG6BGNZP.
    PhylomeDBiQ79FX6.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR003333. Mycolic_cyclopropane_synthase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF02353. CMAS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF003085. CMAS. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q79FX6-1 [UniParc]FASTAAdd to Basket

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    MVNDLTPHFE DVQAHYDLSD DFFRLFLDPT QTYSCAHFER EDMTLEEAQI    50
    AKIDLALGKL GLQPGMTLLD IGCGWGATMR RAIAQYDVNV VGLTLSKNQA 100
    AHVQKSFDEM DTPRDRRVLL AGWEQFNEPV DRIVSIGAFE HFGHDRHADF 150
    FARAHKILPP DGVLLLHTIT GLTRQQMVDH GLPLTLWLAR FLKFIATEIF 200
    PGGQPPTIEM VEEQSAKTGF TLTRRQSLQP HYARTLDLWA EALQEHKSEA 250
    IAIQSEEVYE RYMKYLTGCA KLFRVGYIDV NQFTLAK 287
    Length:287
    Mass (Da):32,724
    Last modified:July 5, 2004 - v1
    Checksum:i669C3224C6B178C0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP43387.1.
    RefSeqiNP_215158.1. NC_000962.3.
    YP_006513985.1. NC_018143.2.

    Genome annotation databases

    EnsemblBacteriaiCCP43387; CCP43387; Rv0644c.
    GeneIDi13318530.
    888061.
    KEGGimtu:Rv0644c.
    mtv:RVBD_0644c.
    PATRICi18149942. VBIMycTub87468_0719.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP43387.1 .
    RefSeqi NP_215158.1. NC_000962.3.
    YP_006513985.1. NC_018143.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TPY X-ray 2.20 A 1-287 [» ]
    ProteinModelPortali Q79FX6.
    SMRi Q79FX6. Positions 3-287.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 83332.Rv0644c.

    Proteomic databases

    PRIDEi Q79FX6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CCP43387 ; CCP43387 ; Rv0644c .
    GeneIDi 13318530.
    888061.
    KEGGi mtu:Rv0644c.
    mtv:RVBD_0644c.
    PATRICi 18149942. VBIMycTub87468_0719.

    Organism-specific databases

    TubercuListi Rv0644c.

    Phylogenomic databases

    eggNOGi COG2230.
    HOGENOMi HOG000245191.
    KOi K00574.
    OMAi KDRQYSC.
    OrthoDBi EOG6BGNZP.
    PhylomeDBi Q79FX6.

    Enzyme and pathway databases

    UniPathwayi UPA00915 .
    BioCyci MetaCyc:RV0644C-MONOMER.
    MTBRV:RV0644C-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q79FX6.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR003333. Mycolic_cyclopropane_synthase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF02353. CMAS. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF003085. CMAS. 1 hit.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Strain: ATCC 25618 / H37Rv.
    8. "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.

    Entry informationi

    Entry nameiMMAA2_MYCTU
    AccessioniPrimary (citable) accession number: Q79FX6
    Secondary accession number(s): L0T7B6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3