MSHA_CORGL
ID MSHA_CORGL Reviewed; 418 AA.
AC Q8NTA6; Q6M7W1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=Cgl0401, cg0481;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP UDP; 1D-INOSITOL 3-PHOSPHATE AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME KINETICS, REACTION MECHANISM, AND
RP SUBUNIT.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=18390549; DOI=10.1074/jbc.m801017200;
RA Vetting M.W., Frantom P.A., Blanchard J.S.;
RT "Structural and enzymatic analysis of MshA from Corynebacterium glutamicum:
RT substrate-assisted catalysis.";
RL J. Biol. Chem. 283:15834-15844(2008).
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:0000269|PubMed:18390549}.
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;
CC Evidence={ECO:0000269|PubMed:18390549};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.21 mM for UDP-GlcNAc {ECO:0000269|PubMed:18390549};
CC KM=0.24 mM for 1D-inositol 3-phosphate {ECO:0000269|PubMed:18390549};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18390549}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. MshA
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF19117.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000036; BAB97794.1; -; Genomic_DNA.
DR EMBL; BX927149; CAF19117.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_599648.1; NC_003450.3.
DR RefSeq; WP_011013628.1; NC_006958.1.
DR PDB; 3C48; X-ray; 2.10 A; A/B=1-418.
DR PDB; 3C4Q; X-ray; 2.80 A; A/B=1-418.
DR PDB; 3C4V; X-ray; 2.60 A; A/B=1-418.
DR PDBsum; 3C48; -.
DR PDBsum; 3C4Q; -.
DR PDBsum; 3C4V; -.
DR AlphaFoldDB; Q8NTA6; -.
DR SMR; Q8NTA6; -.
DR STRING; 196627.cg0481; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR DNASU; 1021208; -.
DR KEGG; cgb:cg0481; -.
DR KEGG; cgl:Cgl0401; -.
DR PATRIC; fig|196627.13.peg.401; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_009583_2_3_11; -.
DR OMA; HTMAKVK; -.
DR BioCyc; MetaCyc:G18NG-9958-MON; -.
DR BRENDA; 2.4.1.250; 960.
DR EvolutionaryTrace; Q8NTA6; -.
DR Proteomes; UP000000582; 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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..418
FT /note="D-inositol 3-phosphate glycosyltransferase"
FT /id="PRO_0000399823"
FT BINDING 9
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT BINDING 15..16
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT BINDING 20..25
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT BINDING 23
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT BINDING 78
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT BINDING 110
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT BINDING 134
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT BINDING 154
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT BINDING 231
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT BINDING 236
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT BINDING 294
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 316
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT BINDING 324
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 85..99
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 110..124
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 149..164
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3C48"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:3C48"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:3C48"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:3C48"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:3C48"
FT HELIX 372..407
FT /evidence="ECO:0007829|PDB:3C48"
SQ SEQUENCE 418 AA; 45669 MW; 3865B32C25DB6C07 CRC64;
MRVAMISMHT SPLQQPGTGD SGGMNVYILS TATELAKQGI EVDIYTRATR PSQGEIVRVA
ENLRVINIAA GPYEGLSKEE LPTQLAAFTG GMLSFTRREK VTYDLIHSHY WLSGQVGWLL
RDLWRIPLIH TAHTLAAVKN SYRDDSDTPE SEARRICEQQ LVDNADVLAV NTQEEMQDLM
HHYDADPDRI SVVSPGADVE LYSPGNDRAT ERSRRELGIP LHTKVVAFVG RLQPFKGPQV
LIKAVAALFD RDPDRNLRVI ICGGPSGPNA TPDTYRHMAE ELGVEKRIRF LDPRPPSELV
AVYRAADIVA VPSFNESFGL VAMEAQASGT PVIAARVGGL PIAVAEGETG LLVDGHSPHA
WADALATLLD DDETRIRMGE DAVEHARTFS WAATAAQLSS LYNDAIANEN VDGETHHG
