ID   MPG1_KLULA              Reviewed;         361 AA.
AC   Q70SJ2; Q6CPE9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Mannose-1-phosphate guanyltransferase;
DE            EC=2.7.7.13;
DE   AltName: Full=GDP-mannose pyrophosphorylase;
DE   AltName: Full=GTP-mannose-1-phosphate guanylyltransferase;
GN   Name=MPG1; Synonyms=PSA1; OrderedLocusNames=KLLA0E05379g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX   PubMed=15851102; DOI=10.1016/j.femsyr.2005.01.004;
RA   Uccelletti D., Staneva D., Rufini S., Venkov P., Palleschi C.;
RT   "Enhanced secretion of heterologous proteins in Kluyveromyces lactis by
RT   overexpression of the GDP-mannose pyrophosphorylase, KlPsa1p.";
RL   FEMS Yeast Res. 5:735-746(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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:15851102};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ551274; CAD82901.1; -; Genomic_DNA.
DR   EMBL; CR382125; CAG99277.1; -; Genomic_DNA.
DR   RefSeq; XP_454190.1; XM_454190.1.
DR   AlphaFoldDB; Q70SJ2; -.
DR   SMR; Q70SJ2; -.
DR   STRING; 28985.XP_454190.1; -.
DR   PRIDE; Q70SJ2; -.
DR   EnsemblFungi; CAG99277; CAG99277; KLLA0_E05435g.
DR   GeneID; 2894004; -.
DR   KEGG; kla:KLLA0_E05435g; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   HOGENOM; CLU_029499_0_0_1; -.
DR   InParanoid; Q70SJ2; -.
DR   OMA; PFLTHQL; -.
DR   UniPathway; UPA00126; UER00930.
DR   Proteomes; UP000000598; Chromosome E.
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; 2.
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"
FT                   /id="PRO_0000238490"
SQ   SEQUENCE   361 AA;  39320 MW;  6EB2DF5CDCA2148C CRC64;
     MKGLILVGGY GTRLRPLTLT VPKPLVEFGN RPMILHQIEA LAAAGVTDIV LAVNYRPEVM
     VETLKKYEDE FGVSITFSVE TEPLGTAGPL KLAESVLKKD NSPFFVLNSD VICDYPFKEL
     ADFHQAHGGK GTIVATKVDE PSKYGVIVHD IATPNLIDRF VEKPVEFVGN RINAGLYILN
     PEVIDLIDLK PTSIEKETFP ILVEQKSLYS FDLEGYWMDV GQPKDFLSGT VLYLNSLSKR
     DPAKLAKGEN IVGNVLVDPT AKISPTAKVG PDVVIGPNVV IGDGVRITRS VALSNSHIKD
     HALVKSTIIG WNSTVGKWAR LEGVTVLGDD VEVKDEIYIN GGKVLPHKSI SVNVPKEAII
     M