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Protein

D-inositol 3-phosphate glycosyltransferase

Gene

mshA

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway.1 Publication

Catalytic activityi

UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate = UDP + 1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol 3-phosphate.1 Publication

Kineticsi

  1. KM=0.21 mM for UDP-GlcNAc1 Publication
  2. KM=0.24 mM for 1D-inositol 3-phosphate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 911D-inositol 3-phosphate
    Binding sitei23 – 231UDP-GlcNAc; via amide nitrogen
    Binding sitei78 – 7811D-inositol 3-phosphate
    Binding sitei110 – 11011D-inositol 3-phosphate
    Binding sitei134 – 13411D-inositol 3-phosphate
    Binding sitei154 – 15411D-inositol 3-phosphate
    Binding sitei231 – 2311UDP-GlcNAc
    Binding sitei236 – 2361UDP-GlcNAc
    Binding sitei294 – 2941UDP-GlcNAc; via amide nitrogen and carbonyl oxygen
    Metal bindingi303 – 3031Magnesium; via carbonyl oxygen
    Metal bindingi304 – 3041Magnesium; via carbonyl oxygen
    Metal bindingi306 – 3061Magnesium; via carbonyl oxygen
    Binding sitei316 – 3161UDP-GlcNAc
    Binding sitei324 – 3241UDP-GlcNAc
    Metal bindingi330 – 3301Magnesium

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-9661.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-inositol 3-phosphate glycosyltransferase (EC:2.4.1.250)
    Alternative name(s):
    N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase
    Short name:
    GlcNAc-Ins-P N-acetylglucosaminyltransferase
    Gene namesi
    Name:mshA
    Ordered Locus Names:Cgl0401, cg0481
    OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
    Taxonomic identifieri196627 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
    Proteomesi
    • UP000000582 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 418418D-inositol 3-phosphate glycosyltransferasePRO_0000399823Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi196627.NCgl0389.

    Structurei

    Secondary structure

    1
    418
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65Combined sources
    Helixi24 – 3714Combined sources
    Beta strandi41 – 477Combined sources
    Helixi51 – 533Combined sources
    Beta strandi55 – 606Combined sources
    Beta strandi63 – 686Combined sources
    Beta strandi73 – 753Combined sources
    Helixi78 – 847Combined sources
    Helixi85 – 9915Combined sources
    Beta strandi104 – 1096Combined sources
    Helixi110 – 12415Combined sources
    Beta strandi128 – 1314Combined sources
    Helixi136 – 1394Combined sources
    Helixi149 – 16416Combined sources
    Beta strandi166 – 1727Combined sources
    Helixi173 – 18311Combined sources
    Helixi187 – 1893Combined sources
    Beta strandi190 – 1923Combined sources
    Turni199 – 2013Combined sources
    Helixi211 – 2166Combined sources
    Beta strandi221 – 23010Combined sources
    Helixi234 – 2363Combined sources
    Helixi238 – 25114Combined sources
    Beta strandi256 – 2627Combined sources
    Helixi274 – 2818Combined sources
    Turni285 – 2873Combined sources
    Beta strandi288 – 2914Combined sources
    Helixi296 – 30510Combined sources
    Beta strandi307 – 3115Combined sources
    Helixi320 – 3278Combined sources
    Beta strandi332 – 3365Combined sources
    Helixi340 – 3434Combined sources
    Turni346 – 3483Combined sources
    Beta strandi349 – 3557Combined sources
    Helixi358 – 37013Combined sources
    Helixi372 – 40736Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3C48X-ray2.10A/B1-418[»]
    3C4QX-ray2.80A/B1-418[»]
    3C4VX-ray2.60A/B1-418[»]
    ProteinModelPortaliQ8NTA6.
    SMRiQ8NTA6. Positions 1-409.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8NTA6.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni15 – 162UDP-GlcNAc binding
    Regioni20 – 2561D-inositol 3-phosphate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4107R5M. Bacteria.
    COG0438. LUCA.
    HOGENOMiHOG000077288.
    KOiK15521.
    OMAiHTMAKVK.
    OrthoDBiEOG647TVR.

    Family and domain databases

    HAMAPiMF_01695. MshA.
    InterProiIPR001296. Glyco_trans_1.
    IPR028098. Glyco_trans_4-like_N.
    IPR017814. Mycothiol_biosynthesis_MshA.
    [Graphical view]
    PfamiPF13439. Glyco_transf_4. 1 hit.
    PF00534. Glycos_transf_1. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR03449. mycothiol_MshA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8NTA6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRVAMISMHT SPLQQPGTGD SGGMNVYILS TATELAKQGI EVDIYTRATR
    60 70 80 90 100
    PSQGEIVRVA ENLRVINIAA GPYEGLSKEE LPTQLAAFTG GMLSFTRREK
    110 120 130 140 150
    VTYDLIHSHY WLSGQVGWLL RDLWRIPLIH TAHTLAAVKN SYRDDSDTPE
    160 170 180 190 200
    SEARRICEQQ LVDNADVLAV NTQEEMQDLM HHYDADPDRI SVVSPGADVE
    210 220 230 240 250
    LYSPGNDRAT ERSRRELGIP LHTKVVAFVG RLQPFKGPQV LIKAVAALFD
    260 270 280 290 300
    RDPDRNLRVI ICGGPSGPNA TPDTYRHMAE ELGVEKRIRF LDPRPPSELV
    310 320 330 340 350
    AVYRAADIVA VPSFNESFGL VAMEAQASGT PVIAARVGGL PIAVAEGETG
    360 370 380 390 400
    LLVDGHSPHA WADALATLLD DDETRIRMGE DAVEHARTFS WAATAAQLSS
    410
    LYNDAIANEN VDGETHHG
    Length:418
    Mass (Da):45,669
    Last modified:October 1, 2002 - v1
    Checksum:i3865B32C25DB6C07
    GO

    Sequence cautioni

    The sequence CAF19117.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000036 Genomic DNA. Translation: BAB97794.1.
    BX927149 Genomic DNA. Translation: CAF19117.1. Different initiation.
    RefSeqiNP_599648.1. NC_003450.3.
    WP_011013628.1. NC_006958.1.

    Genome annotation databases

    EnsemblBacteriaiBAB97794; BAB97794; BAB97794.
    CAF19117; CAF19117; cg0481.
    GeneIDi1021208.
    KEGGicgb:cg0481.
    cgl:NCgl0389.
    PATRICi21492860. VBICorGlu203724_0401.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000036 Genomic DNA. Translation: BAB97794.1.
    BX927149 Genomic DNA. Translation: CAF19117.1. Different initiation.
    RefSeqiNP_599648.1. NC_003450.3.
    WP_011013628.1. NC_006958.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3C48X-ray2.10A/B1-418[»]
    3C4QX-ray2.80A/B1-418[»]
    3C4VX-ray2.60A/B1-418[»]
    ProteinModelPortaliQ8NTA6.
    SMRiQ8NTA6. Positions 1-409.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi196627.NCgl0389.

    Protocols and materials databases

    DNASUi1021208.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAB97794; BAB97794; BAB97794.
    CAF19117; CAF19117; cg0481.
    GeneIDi1021208.
    KEGGicgb:cg0481.
    cgl:NCgl0389.
    PATRICi21492860. VBICorGlu203724_0401.

    Phylogenomic databases

    eggNOGiENOG4107R5M. Bacteria.
    COG0438. LUCA.
    HOGENOMiHOG000077288.
    KOiK15521.
    OMAiHTMAKVK.
    OrthoDBiEOG647TVR.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-9661.

    Miscellaneous databases

    EvolutionaryTraceiQ8NTA6.

    Family and domain databases

    HAMAPiMF_01695. MshA.
    InterProiIPR001296. Glyco_trans_1.
    IPR028098. Glyco_trans_4-like_N.
    IPR017814. Mycothiol_biosynthesis_MshA.
    [Graphical view]
    PfamiPF13439. Glyco_transf_4. 1 hit.
    PF00534. Glycos_transf_1. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR03449. mycothiol_MshA. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
      Ikeda M., Nakagawa S.
      Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    3. "Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis."
      Vetting M.W., Frantom P.A., Blanchard J.S.
      J. Biol. Chem. 283:15834-15844(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH UDP; 1D-INOSITOL 3-PHOSPHATE AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME KINETICS, REACTION MECHANISM, SUBUNIT.
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

    Entry informationi

    Entry nameiMSHA_CORGL
    AccessioniPrimary (citable) accession number: Q8NTA6
    Secondary accession number(s): Q6M7W1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: October 1, 2002
    Last modified: May 11, 2016
    This is version 78 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.