ID MSHA_MYCTU Reviewed; 480 AA.
AC P64707; L0T3R4; Q11152;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 01-MAY-2013, entry version 53.
DE RecName: Full=D-inositol 3-phosphate glycosyltransferase;
DE EC=2.4.1.250;
DE AltName: Full=N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase;
DE Short=GlcNAc-Ins-P N-acetylglucosaminyltransferase;
GN Name=mshA; OrderedLocusNames=Rv0486, MT0504; ORFNames=MTCY20G9.12;
OS Mycobacterium tuberculosis.
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the
RT complete genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [3]
RP FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12754249; DOI=10.1128/JB.185.11.3476-3479.2003;
RA Newton G.L., Koledin T., Gorovitz B., Rawat M., Fahey R.C., Av-Gay Y.;
RT "The glycosyltransferase gene encoding the enzyme catalyzing the first
RT step of mycothiol biosynthesis (mshA).";
RL J. Bacteriol. 185:3476-3479(2003).
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.
CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + 1D-myo-inositol
CC 3-phosphate = UDP + 1-O-(2-acetamido-2-deoxy-alpha-D-
CC glucopyranosyl)-1D-myo-inositol 3-phosphate.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC MshA subfamily.
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DR EMBL; BX842573; CAB00947.1; -; Genomic_DNA.
DR EMBL; AE000516; AAK44727.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43220.1; -; Genomic_DNA.
DR PIR; A70744; A70744.
DR RefSeq; NP_215000.1; NC_000962.3.
DR RefSeq; NP_334913.1; NC_002755.2.
DR RefSeq; YP_006513816.1; NC_018143.1.
DR ProteinModelPortal; P64707; -.
DR SMR; P64707; 46-446.
DR STRING; 83332.Rv0486; -.
DR EnsemblBacteria; AAK44727; AAK44727; MT0504.
DR GeneID; 13318357; -.
DR GeneID; 887160; -.
DR GeneID; 923860; -.
DR KEGG; mtc:MT0504; -.
DR KEGG; mtu:Rv0486; -.
DR KEGG; mtv:RVBD_0486; -.
DR PATRIC; 18122814; VBIMycTub22151_0541.
DR TubercuList; Rv0486; -.
DR eggNOG; COG0438; -.
DR HOGENOM; HOG000077288; -.
DR KO; K15521; -.
DR OMA; FAGRIQP; -.
DR ProtClustDB; CLSK871811; -.
DR Reactome; REACT_27295; Mycobacterium tuberculosis biological processes.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0010125; P:mycothiol biosynthetic process; IMP:MTBBASE.
DR HAMAP; MF_01695; MshA; 1; -.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR017814; Mycothiol_biosynthesis_MshA.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR03449; mycothiol_MshA; 1.
PE 3: Inferred from homology;
KW Complete proteome; Glycosyltransferase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1 480 D-inositol 3-phosphate
FT glycosyltransferase.
FT /FTId=PRO_0000080318.
FT REGION 59 60 UDP-GlcNAc binding (By similarity).
FT REGION 64 69 1D-inositol 3-phosphate binding (By
FT similarity).
FT METAL 340 340 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 341 341 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 343 343 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 367 367 Magnesium (By similarity).
FT BINDING 53 53 1D-inositol 3-phosphate (By similarity).
FT BINDING 67 67 UDP-GlcNAc; via amide nitrogen (By
FT similarity).
FT BINDING 122 122 1D-inositol 3-phosphate (By similarity).
FT BINDING 155 155 1D-inositol 3-phosphate (By similarity).
FT BINDING 179 179 1D-inositol 3-phosphate (By similarity).
FT BINDING 199 199 1D-inositol 3-phosphate (By similarity).
FT BINDING 273 273 UDP-GlcNAc (By similarity).
FT BINDING 278 278 UDP-GlcNAc (By similarity).
FT BINDING 331 331 UDP-GlcNAc; via amide nitrogen and
FT carbonyl oxygen (By similarity).
FT BINDING 353 353 UDP-GlcNAc (By similarity).
FT BINDING 361 361 UDP-GlcNAc (By similarity).
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
//
