(data stored in ACNUC30630 zone)

SWISSPROT: MSHA_CORGB

ID   MSHA_CORGB              Reviewed;         418 AA.
AC   A4QB40;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   11-DEC-2019, entry version 69.
DE   RecName: Full=D-inositol 3-phosphate glycosyltransferase;
DE            EC=2.4.1.250 {ECO:0000255|HAMAP-Rule:MF_01695};
DE   AltName: Full=N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_01695};
DE            Short=GlcNAc-Ins-P N-acetylglucosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_01695};
GN   Name=mshA {ECO:0000255|HAMAP-Rule:MF_01695}; OrderedLocusNames=cgR_0473;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(2007).
CC   -!- FUNCTION: Catalyzes the transfer of a N-acetyl-glucosamine moiety to
CC       1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-
CC       deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis
CC       pathway. {ECO:0000255|HAMAP-Rule:MF_01695}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 3-phosphate + UDP-N-acetyl-alpha-D-glucosamine
CC         = 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside 3-
CC         phosphate + H(+) + UDP; Xref=Rhea:RHEA:26188, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58401,
CC         ChEBI:CHEBI:58892; EC=2.4.1.250; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01695};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01695}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. MshA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01695}.
DR   EMBL; AP009044; BAF53437.1; -; Genomic_DNA.
DR   RefSeq; WP_011013628.1; NC_009342.1.
DR   SMR; A4QB40; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblBacteria; BAF53437; BAF53437; cgR_0473.
DR   KEGG; cgt:cgR_0473; -.
DR   HOGENOM; HOG000077288; -.
DR   KO; K15521; -.
DR   OMA; HTMAKVK; -.
DR   BioCyc; CGLU340322:G1G2L-498-MONOMER; -.
DR   Proteomes; UP000006698; Chromosome.
DR   GO; GO:0008375; F:acetylglucosaminyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102710; F:D-inositol-3-phosphate glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010125; P:mycothiol biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01695; MshA; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   InterPro; IPR017814; Mycothiol_biosynthesis_MshA.
DR   Pfam; PF13439; Glyco_transf_4; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   TIGRFAMs; TIGR03449; mycothiol_MshA; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4QB40.
DR   SWISS-2DPAGE; A4QB40.
KW   Glycosyltransferase; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..418
FT                   /note="D-inositol 3-phosphate glycosyltransferase"
FT                   /id="PRO_0000400118"
FT   REGION          15..16
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   REGION          20..25
FT                   /note="1D-inositol 3-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   METAL           303
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   METAL           304
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   METAL           306
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   METAL           330
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         9
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         23
FT                   /note="UDP-GlcNAc; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         78
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         110
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         134
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         154
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         231
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         236
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         294
FT                   /note="UDP-GlcNAc; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         316
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         324
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
SQ   SEQUENCE   418 AA;  45669 MW;  3865B32C25DB6C07 CRC64;
     MRVAMISMHT SPLQQPGTGD SGGMNVYILS TATELAKQGI EVDIYTRATR PSQGEIVRVA
     ENLRVINIAA GPYEGLSKEE LPTQLAAFTG GMLSFTRREK VTYDLIHSHY WLSGQVGWLL
     RDLWRIPLIH TAHTLAAVKN SYRDDSDTPE SEARRICEQQ LVDNADVLAV NTQEEMQDLM
     HHYDADPDRI SVVSPGADVE LYSPGNDRAT ERSRRELGIP LHTKVVAFVG RLQPFKGPQV
     LIKAVAALFD RDPDRNLRVI ICGGPSGPNA TPDTYRHMAE ELGVEKRIRF LDPRPPSELV
     AVYRAADIVA VPSFNESFGL VAMEAQASGT PVIAARVGGL PIAVAEGETG LLVDGHSPHA
     WADALATLLD DDETRIRMGE DAVEHARTFS WAATAAQLSS LYNDAIANEN VDGETHHG
//

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