ID   MPG11_CANGA             Reviewed;         361 AA.
AC   Q9Y725; Q6FWD5;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Mannose-1-phosphate guanyltransferase 1;
DE            EC=2.7.7.13;
DE   AltName: Full=ATP-mannose-1-phosphate guanylyltransferase 1;
DE   AltName: Full=GDP-mannose pyrophosphorylase 1;
GN   Name=MPG1; Synonyms=VIG9; OrderedLocusNames=CAGL0D01034g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=10913825; DOI=10.1016/s0304-4165(00)00075-1;
RA   Ohta A., Chibana H., Arisawa M., Sudoh M.;
RT   "The VIG9 gene products from the human pathogenic fungi Candida albicans
RT   and Candida glabrata encode GDP-mannose pyrophosphorylase.";
RL   Biochim. Biophys. Acta 1475:265-272(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Involved in cell wall synthesis where it is required for
CC       glycosylation. Involved in cell cycle progression through cell-size
CC       checkpoint (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC         alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
CC         ChEBI:CHEBI:58409; EC=2.7.7.13;
CC         Evidence={ECO:0000269|PubMed:10913825};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC       route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
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DR   EMBL; AB020570; BAA77382.1; -; Genomic_DNA.
DR   EMBL; CR380950; CAG58370.1; -; Genomic_DNA.
DR   RefSeq; XP_445459.1; XM_445459.1.
DR   AlphaFoldDB; Q9Y725; -.
DR   SMR; Q9Y725; -.
DR   STRING; 5478.XP_445459.1; -.
DR   EnsemblFungi; CAG58370; CAG58370; CAGL0D01034g.
DR   GeneID; 2886966; -.
DR   KEGG; cgr:CAGL0D01034g; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   HOGENOM; CLU_029499_0_0_1; -.
DR   BRENDA; 2.7.7.13; 1113.
DR   UniPathway; UPA00126; UER00930.
DR   Proteomes; UP000002428; Chromosome D.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006486; P:protein glycosylation; IEA:EnsemblFungi.
DR   CDD; cd06425; M1P_guanylylT_B_like_N; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR045233; GMPPB_N.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 3.
PE   1: Evidence at protein level;
KW   Cell cycle; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..361
FT                   /note="Mannose-1-phosphate guanyltransferase 1"
FT                   /id="PRO_0000238485"
FT   CONFLICT        55
FT                   /note="C -> Y (in Ref. 2; CAG58370)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        330
FT                   /note="N -> D (in Ref. 2; CAG58370)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   361 AA;  39299 MW;  E255084D2EDB2A1D CRC64;
     MKGLILVGGY GTRLRPLTLT VPKPLVEFGN RPMILHQIEA LANAGVTDIV LAVNCRPEVM
     VETLQKYEKE YGVSITFSVE TEPLGTAGPL KLAEKVLKKD NSPFFVLNSD VICEYPFKEL
     ADFHKAHGGK GTIVATKVDE PSKYGVIVHD IATPNLIDRF VEKPKEFVGN RINAGLYILN
     PEVIDLIEMK PTSIETETFP ILVEQKSLYS FDLEGFWMDV GQPKDFLSGT VLYLNSVSKK
     NPEKLTKGDN IVGNVMVDPS AKIAASAKVG PDVVIGPNVT IGEGVRITRS VVLSDSSIQD
     HSLVKSTIVG WKSTVGKWCR LEGVTVLGDN VVVKDEVYVN GGKVLPHKSI SANVPSEAII
     M