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Database: UniProt
Entry: A0A059MLQ9_9NOCA
LinkDB: A0A059MLQ9_9NOCA
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ID   A0A059MLQ9_9NOCA        Unreviewed;       445 AA.
AC   A0A059MLQ9; A0A0F6VKX0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   16-JAN-2019, entry version 27.
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=N505_0116835 {ECO:0000313|EMBL:KDE11962.1};
OS   Rhodococcus aetherivorans.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=191292 {ECO:0000313|EMBL:KDE11962.1, ECO:0000313|Proteomes:UP000024941};
RN   [1] {ECO:0000313|EMBL:KDE11962.1, ECO:0000313|Proteomes:UP000024941}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCP1 {ECO:0000313|EMBL:KDE11962.1,
RC   ECO:0000313|Proteomes:UP000024941};
RX   PubMed=24158549;
RA   Cappelletti M., Di Gennaro P., D'Ursi P., Orro A., Mezzelani A.,
RA   Landini M., Fedi S., Frascari D., Presentato A., Zannoni D.,
RA   Milanesi L.;
RT   "Genome Sequence of Rhodococcus sp. Strain BCP1, a Biodegrader of
RT   Alkanes and Chlorinated Compounds.";
RL   Genome Announc. 1:e00657-13(2013).
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:KDE11962.1}.
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DR   EMBL; AVAE01000021; KDE11962.1; -; Genomic_DNA.
DR   RefSeq; WP_006936015.1; NZ_CP011341.1.
DR   EnsemblBacteria; KDE11962; KDE11962; N505_0116835.
DR   GeneID; 29565807; -.
DR   KEGG; rav:AAT18_19425; -.
DR   PATRIC; fig|191292.16.peg.3450; -.
DR   KO; K15521; -.
DR   Proteomes; UP000024941; 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   Complete proteome {ECO:0000313|Proteomes:UP000024941};
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:UP000024941};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01695,
KW   ECO:0000256|SAAS:SAAS00548568, ECO:0000313|EMBL:KDE11962.1}.
FT   DOMAIN       30    211       Glyco_trans_4-like_N. {ECO:0000259|Pfam:
FT                                PF13439}.
FT   DOMAIN      218    391       Glycos_transf_1. {ECO:0000259|Pfam:
FT                                PF00534}.
FT   REGION       24     25       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01695}.
FT   REGION       29     34       1D-inositol 3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   METAL       311    311       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   METAL       312    312       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   METAL       314    314       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   METAL       338    338       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01695}.
FT   BINDING      18     18       1D-inositol 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   BINDING      32     32       UDP-GlcNAc; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   BINDING      87     87       1D-inositol 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   BINDING     120    120       1D-inositol 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   BINDING     144    144       1D-inositol 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   BINDING     164    164       1D-inositol 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01695}.
FT   BINDING     238    238       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01695}.
FT   BINDING     243    243       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01695}.
FT   BINDING     302    302       UDP-GlcNAc; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01695}.
FT   BINDING     324    324       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01695}.
FT   BINDING     332    332       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01695}.
SQ   SEQUENCE   445 AA;  47113 MW;  3A9124429DE9DF6A CRC64;
     MTSKSNSRPR RVAVLSVHTS PLAQPGTGDA GGMNVYVLQT AVQLARRGVE VEIFTRATSS
     ADPVVQEAAP GVLVRNVAAG PYEGLDKHDL PTQLCAFAAG VLREEARHPQ GYYDLVHSHY
     WLSGQVGWLA RDRWGVPLVH TAHTLAAVKN ASLADGDVPE PAARQIGEQQ VVAESDRLVA
     NTVDEAAQLE RSYGADPSRV DVVAPGADLS RYRPGDRAAA RAGLGLDPRE TIVTFVGRIQ
     PLKAPDVLLR AAAAAMSADP EVPLRVLVVG GPSGTGLERP HSLIELAAEL GIAARVTFLP
     PQPPERLVQV YRASDVVAVP SYSESFGLVA IEAQACGTPV LAANVGGLGV AVRDGETGLL
     VDGHRTDDWA AALRALVTDP GRRAALAAAA PLHAENFSWE HTAEGLLASY RKAGALRNRS
     LGTGEFPLRR QRGVWKIRRT TGVRA
//
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