(data stored in ACNUC7421 zone)

SWISSPROT: MSHA_MYCTK

ID   MSHA_MYCTK              Reviewed;         480 AA.
AC   C6DT68;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   08-MAY-2019, entry version 54.
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};
GN   OrderedLocusNames=TBMG_00489;
OS   Mycobacterium tuberculosis (strain KZN 1435 / MDR).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=478434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KZN 1435 / MDR;
RA   Murray M., Pillay M., Borowsky M.L., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J.,
RA   Yandava C., Haas B., Nusbaum C., Galagan J., Birren B.;
RT   "The genome sequence of Mycobacterium tuberculosis strain KZN 1435.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a N-acetyl-glucosamine moiety
CC       to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-
CC       acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol
CC       (MSH) biosynthesis pathway (By similarity). MSH and WhiB3 are
CC       probably part of a regulatory circuit that mediates gene
CC       expression upon acid stress (like that found in host macrophage
CC       phagosomes). MSH is one of the major redox buffers which protects
CC       bacteria against redox stressors and antibiotics; loss of MSH or
CC       ergothioneine (ERG, the other major redox buffer in this bacteria)
CC       leads to respiratory alterations and bioenergetic deficiencies
CC       that negatively impact virulence (By similarity).
CC       {ECO:0000250|UniProtKB:P9WMY7, ECO:0000255|HAMAP-Rule:MF_01695}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 3-phosphate + UDP-N-acetyl-alpha-D-
CC         glucosamine = 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-
CC         glucopyranoside 3-phosphate + H(+) + UDP; Xref=Rhea:RHEA:26188,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58401, ChEBI:CHEBI:58892; EC=2.4.1.250;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01695};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01695}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       MshA subfamily. {ECO:0000255|HAMAP-Rule:MF_01695}.
DR   EMBL; CP001658; ACT23520.1; -; Genomic_DNA.
DR   RefSeq; WP_003402367.1; NZ_KK341220.1.
DR   SMR; C6DT68; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblBacteria; ACT23520; ACT23520; TBMG_00489.
DR   KEGG; mtb:TBMG_00489; -.
DR   PATRIC; fig|478434.13.peg.3755; -.
DR   HOGENOM; HOG000077288; -.
DR   KO; K15521; -.
DR   OMA; HTMAKVK; -.
DR   BioCyc; MTUB478434:G1GF9-514-MONOMER; -.
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; C6DT68.
DR   SWISS-2DPAGE; C6DT68.
KW   Glycosyltransferase; Magnesium; Metal-binding; Transferase.
FT   CHAIN         1    480       D-inositol 3-phosphate
FT                                glycosyltransferase.
FT                                /FTId=PRO_0000400143.
FT   REGION       59     60       UDP-GlcNAc binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01695}.
FT   REGION       64     69       1D-inositol 3-phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01695}.
FT   METAL       340    340       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01695}.
FT   METAL       341    341       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01695}.
FT   METAL       343    343       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01695}.
FT   METAL       367    367       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01695}.
FT   BINDING      53     53       1D-inositol 3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01695}.
FT   BINDING      67     67       UDP-GlcNAc; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01695}.
FT   BINDING     122    122       1D-inositol 3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01695}.
FT   BINDING     155    155       1D-inositol 3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01695}.
FT   BINDING     179    179       1D-inositol 3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01695}.
FT   BINDING     199    199       1D-inositol 3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01695}.
FT   BINDING     273    273       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01695}.
FT   BINDING     278    278       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01695}.
FT   BINDING     331    331       UDP-GlcNAc; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01695}.
FT   BINDING     353    353       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01695}.
FT   BINDING     361    361       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01695}.
SQ   SEQUENCE   480 AA;  50541 MW;  2134755E894A9CCF CRC64;
     MAGVRHDDGS GLIAQRRPVR GEGATRSRGP SGPSNRNVSA ADDPRRVALL AVHTSPLAQP
     GTGDAGGMNV YMLQSALHLA RRGIEVEIFT RATASADPPV VRVAPGVLVR NVVAGPFEGL
     DKYDLPTQLC AFAAGVLRAE AVHEPGYYDI VHSHYWLSGQ VGWLARDRWA VPLVHTAHTL
     AAVKNAALAD GDGPEPPLRT VGEQQVVDEA DRLIVNTDDE ARQVISLHGA DPARIDVVHP
     GVDLDVFRPG DRRAARAALG LPVDERVVAF VGRIQPLKAP DIVLRAAAKL PGVRIIVAGG
     PSGSGLASPD GLVRLADELG ISARVTFLPP QSHTDLATLF RAADLVAVPS YSESFGLVAV
     EAQACGTPVV AAAVGGLPVA VRDGITGTLV SGHEVGQWAD AIDHLLRLCA GPRGRVMSRA
     AARHAATFSW ENTTDALLAS YRRAIGEYNA ERQRRGGEVI SDLVAVGKPR HWTPRRGVGA
//

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