(data stored in ACNUC30630 zone)

SWISSPROT: MSHA_MYCSJ

ID   MSHA_MYCSJ              Reviewed;         439 AA.
AC   A3PU84;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 76.
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=Mjls_0650;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) 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 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; CP000580; ABN96461.1; -; Genomic_DNA.
DR   RefSeq; WP_011854536.1; NC_009077.1.
DR   SMR; A3PU84; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblBacteria; ABN96461; ABN96461; Mjls_0650.
DR   KEGG; mjl:Mjls_0650; -.
DR   eggNOG; ENOG4107R5M; Bacteria.
DR   eggNOG; COG0438; LUCA.
DR   HOGENOM; HOG000077288; -.
DR   KO; K15521; -.
DR   OMA; HTMAKVK; -.
DR   BioCyc; MSP164757:G1G8C-657-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; A3PU84.
DR   SWISS-2DPAGE; A3PU84.
KW   Glycosyltransferase; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..439
FT                   /note="D-inositol 3-phosphate glycosyltransferase"
FT                   /id="PRO_0000400138"
FT   REGION          27..28
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   REGION          32..37
FT                   /note="1D-inositol 3-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   METAL           308
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   METAL           309
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   METAL           311
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   METAL           335
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         21
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         35
FT                   /note="UDP-GlcNAc; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         90
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         123
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         147
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         167
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         241
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         246
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         299
FT                   /note="UDP-GlcNAc; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         321
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         329
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
SQ   SEQUENCE   439 AA;  46734 MW;  FC55BF85068630F1 CRC64;
     MRLATDQLGR PPQRVAVLSV HTSPLAQPGT GDAGGMNVYV LQSALHMARR GVEVEIFTRA
     TTSADPPVVR VAPGVLVRNV VAGPFEGLDK YDLPTQLCAF TAGVLRAEAT HEPGYYDIVH
     SHYWLSGQVG WLARDRWAVP LVHTAHTLAA VKNAALAEGD SPEPPLRAVG EQQVVDEADR
     LIVNTELEAE QLVSLHNADP SRIDVVHPGV DLDTFTPGDQ AAARAALGLD PRETVVAFVG
     RIQPLKAPDI LLRAAAKLPD VRVLVAGGPS GSGLAAPDNL VALADELGIS ERVTFLPPQS
     REDLVRVYRA ADLVAVPSYS ESFGLVAVEA QACGTPVVAA AVGGLPVAVR DGVTGALVDG
     HDVGDWAHTI DSLLSRGPAT MRRAAVEHAA TFSWAHTVDD LLASYGRAIS DYRDRHPHAD
     ETLSRRTARR FSRRRGVRA
//

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