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MSHA_MYCLB
ID   MSHA_MYCLB              Reviewed;         428 AA.
AC   B8ZT88;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=MLBr02443;
OS   Mycobacterium leprae (strain Br4923).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=561304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Br4923;
RX   PubMed=19881526; DOI=10.1038/ng.477;
RA   Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA   Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA   Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA   Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA   Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA   Rougemont J., Brennan P.J., Cole S.T.;
RT   "Comparative genomic and phylogeographic analysis of Mycobacterium
RT   leprae.";
RL   Nat. Genet. 41:1282-1289(2009).
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}.
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DR   EMBL; FM211192; CAR72542.1; -; Genomic_DNA.
DR   RefSeq; WP_010908903.1; NC_011896.1.
DR   AlphaFoldDB; B8ZT88; -.
DR   SMR; B8ZT88; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblBacteria; CAR72542; CAR72542; MLBr02443.
DR   KEGG; mlb:MLBr02443; -.
DR   HOGENOM; CLU_009583_2_3_11; -.
DR   OMA; HTMAKVK; -.
DR   OrthoDB; 694191at2; -.
DR   Proteomes; UP000006900; 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;
KW   Glycosyltransferase; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..428
FT                   /note="D-inositol 3-phosphate glycosyltransferase"
FT                   /id="PRO_0000400135"
FT   BINDING         5
FT                   /ligand="1D-myo-inositol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58401"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         11..12
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         16..21
FT                   /ligand="1D-myo-inositol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58401"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         19
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         74
FT                   /ligand="1D-myo-inositol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58401"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         107
FT                   /ligand="1D-myo-inositol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58401"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         131
FT                   /ligand="1D-myo-inositol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58401"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         151
FT                   /ligand="1D-myo-inositol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58401"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         225
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         230
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         283
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         293
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         305
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         313
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         319
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
SQ   SEQUENCE   428 AA;  45292 MW;  A14F9F0187E3587C CRC64;
     MLAVHTSPLA QPGIGDAGGM NVYVLQSALH LARRGIEVEI FTRATASADP PIVWVAPGVL
     VRNVVAGPFE GLDKYDLPTQ LCAFAAGVLR AEAAHEPGYY DIVHSHYWLS GQVGWLARDR
     WAVPLVHTAH TLAAVKNAAL ADGDAAEPPL RSVGEQQVVD EADRMIVNTD DEARQLISIH
     RADPAKIDVA HPGVDLDMFR PGDRRAARAA LGLPLDGNVV AFVGRIQPLK APDIVLRAAA
     KLPQVRIVVA GGPSGSGLAS PDGLVRLADE LGITARVTFL PPQSRTNLAT VFQAADLVAV
     PSYSESFGLV AVEAQACGTP VVAAAVGGLP VAVRDGVTGT LVFGHNVGHW ADAVDQLLRL
     SAGPQARAIS RAAVVHAAQF SWDNTTDALL ASYRRAIGDF TATRQHRVRD LVATRKPRRW
     ISRRGMGA
 
 
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