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Database: UniProt
Entry: W9BLE0_9MYCO
LinkDB: W9BLE0_9MYCO
Original site: W9BLE0_9MYCO 
ID   W9BLE0_9MYCO            Unreviewed;       424 AA.
AC   W9BLE0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   10-APR-2019, entry version 29.
DE   RecName: Full=D-inositol-3-phosphate glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01695};
DE            EC=2.4.1.250 {ECO:0000256|HAMAP-Rule:MF_01695};
DE   AltName: Full=N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_01695};
DE            Short=GlcNAc-Ins-P N-acetylglucosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_01695};
GN   Name=mshA {ECO:0000256|HAMAP-Rule:MF_01695};
GN   ORFNames=BN977_04308 {ECO:0000313|EMBL:CDO09485.1};
OS   Mycolicibacterium cosmeticum.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=258533 {ECO:0000313|EMBL:CDO09485.1, ECO:0000313|Proteomes:UP000028870};
RN   [1] {ECO:0000313|EMBL:CDO09485.1, ECO:0000313|Proteomes:UP000028870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44829 {ECO:0000313|EMBL:CDO09485.1,
RC   ECO:0000313|Proteomes:UP000028870};
RA   Croce O., Robert C., Raoult D., Drancourt M.;
RT   "Draft Genome Sequence of Mycobacterium cosmeticum DSM 44829.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDO09485.1, ECO:0000313|Proteomes:UP000028870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44829 {ECO:0000313|EMBL:CDO09485.1,
RC   ECO:0000313|Proteomes:UP000028870};
RA   Urmite Genomes U.;
RL   Submitted (MAR-2014) 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       biosynthesis pathway. {ECO:0000256|HAMAP-Rule:MF_01695,
CC       ECO:0000256|SAAS:SAAS00722632}.
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:0000256|HAMAP-Rule:MF_01695,
CC         ECO:0000256|SAAS:SAAS01117664};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01695}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       MshA subfamily. {ECO:0000256|HAMAP-Rule:MF_01695,
CC       ECO:0000256|SAAS:SAAS00536841}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CDO09485.1}.
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DR   EMBL; CCBB010000003; CDO09485.1; -; Genomic_DNA.
DR   STRING; 258533.BN977_04308; -.
DR   EnsemblBacteria; CDO09485; CDO09485; BN977_04308.
DR   Proteomes; UP000028870; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000028870};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01695,
KW   ECO:0000256|SAAS:SAAS00548564};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01695,
KW   ECO:0000256|SAAS:SAAS00536904};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01695,
KW   ECO:0000256|SAAS:SAAS00536915};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028870};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01695,
KW   ECO:0000256|SAAS:SAAS00548568, ECO:0000313|EMBL:CDO09485.1}.
FT   DOMAIN       19    199       Glyco_trans_4-like_N. {ECO:0000259|Pfam:
FT                                PF13439}.
FT   DOMAIN      206    368       Glycos_transf_1. {ECO:0000259|Pfam:
FT                                PF00534}.
FT   REGION       13     14       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01695}.
FT   REGION       18     23       1D-inositol 3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   METAL       294    294       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   METAL       295    295       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   METAL       297    297       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   METAL       321    321       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01695}.
FT   BINDING       7      7       1D-inositol 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   BINDING      21     21       UDP-GlcNAc; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   BINDING      76     76       1D-inositol 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   BINDING     109    109       1D-inositol 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   BINDING     133    133       1D-inositol 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   BINDING     153    153       1D-inositol 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   BINDING     227    227       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01695}.
FT   BINDING     232    232       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01695}.
FT   BINDING     285    285       UDP-GlcNAc; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01695}.
FT   BINDING     307    307       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01695}.
FT   BINDING     315    315       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01695}.
SQ   SEQUENCE   424 AA;  44512 MW;  41CC2D41E2F6E867 CRC64;
     MAVLSVHTSP LAQPGTGDAG GMNVYVLQTA LELARRGVDV EIFTRATSSA DEPVVRVAPG
     VLVRNVVAGP FEGLDKNDLP TQLCAFTAGV LRAEANHEPG YYDIVHSHYW LSGQVGWLAR
     DRWAVPLVHT AHTLAAVKNA SLAAGDTPEP ALRAIGEQQV VDEADRLIVN TELEAQQLVS
     LHHASRAQID VVHPGVDLAV FTPGDKRAAR AALGLDPTEP IVAFVGRIQP LKAPDVLLRA
     VAELPRARVV VAGGPSGSGL AAPDGLIRLA DQLGITDRVT FLPPQSRAQL VDVYRAADLV
     AVPSYSESFG LVAVEAQACG TPVVAAAVGG LPVAVRDGVT GALVDGHDPE RWAAVIGALL
     ASGPERLGAA AVAHAATFSW AHTVDALLAG YGRAIADYRA RHPRRDATAR RGGRRFSMRR
     GVRL
//
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