位置:首页 > 蛋白库 > MSHA_MYCTK
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   03-AUG-2022, entry version 64.
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=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., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I., Hepburn T.A.,
RA   Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., 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 to
CC       1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-
CC       deoxy-glucopyranoside 3-phosphate in the mycothiol (MSH) biosynthesis
CC       pathway (By similarity). MSH and WhiB3 are probably part of a
CC       regulatory circuit that mediates gene expression upon acid stress (like
CC       that found in host macrophage phagosomes). MSH is one of the major
CC       redox buffers which protects bacteria against redox stressors and
CC       antibiotics; loss of MSH or ergothioneine (ERG, the other major redox
CC       buffer in this bacteria) leads to respiratory alterations and
CC       bioenergetic deficiencies that negatively impact virulence (By
CC       similarity). {ECO:0000250|UniProtKB:P9WMY7, ECO:0000255|HAMAP-
CC       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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001658; ACT23520.1; -; Genomic_DNA.
DR   RefSeq; WP_003402367.1; NZ_KK341220.1.
DR   AlphaFoldDB; C6DT68; -.
DR   SMR; C6DT68; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   KEGG; mtb:TBMG_00489; -.
DR   PATRIC; fig|478434.13.peg.3755; -.
DR   HOGENOM; CLU_009583_2_3_11; -.
DR   OMA; HTMAKVK; -.
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;
KW   Glycosyltransferase; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..480
FT                   /note="D-inositol 3-phosphate glycosyltransferase"
FT                   /id="PRO_0000400143"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53
FT                   /ligand="1D-myo-inositol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58401"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         59..60
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         64..69
FT                   /ligand="1D-myo-inositol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58401"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         67
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         122
FT                   /ligand="1D-myo-inositol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58401"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         155
FT                   /ligand="1D-myo-inositol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58401"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         179
FT                   /ligand="1D-myo-inositol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58401"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         199
FT                   /ligand="1D-myo-inositol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58401"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         273
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         278
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         331
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         340
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         341
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         343
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         353
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         361
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         367
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024