ID   MPG1_YARLI              Reviewed;         363 AA.
AC   Q6CCU3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
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; OrderedLocusNames=YALI0C06490g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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   -!- 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; CR382129; CAG81822.1; -; Genomic_DNA.
DR   RefSeq; XP_501519.1; XM_501519.1.
DR   AlphaFoldDB; Q6CCU3; -.
DR   SMR; Q6CCU3; -.
DR   STRING; 4952.CAG81822; -.
DR   EnsemblFungi; CAG81822; CAG81822; YALI0_C06490g.
DR   GeneID; 2909316; -.
DR   KEGG; yli:YALI0C06490g; -.
DR   VEuPathDB; FungiDB:YALI0_C06490g; -.
DR   HOGENOM; CLU_029499_0_0_1; -.
DR   InParanoid; Q6CCU3; -.
DR   OMA; PFLTHQL; -.
DR   UniPathway; UPA00126; UER00930.
DR   Proteomes; UP000001300; Chromosome C.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
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; 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.
PE   3: Inferred from homology;
KW   Cell cycle; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..363
FT                   /note="Mannose-1-phosphate guanyltransferase"
FT                   /id="PRO_0000238494"
SQ   SEQUENCE   363 AA;  39767 MW;  63D59D50107F3922 CRC64;
     MKGLILVGGY GTRLRPLTLT LPKPLVEFGN KPMILHQVES LAAAGVKDIV LAVNYRPEVM
     IETLKKYEEK YGVNITFSVE TEPLGTAGPL KLAEEILCKD DTPFFVLNSD VICDYPFAEL
     AEFHKKNNAE ATIVATKVEE PSKYGVIVHK QGTSKIDRFV EKPVEFVGNR INAGIYILNP
     SVVDLIDLRP TSIEKETFPQ LAARESLYSF DLEGYWMDVG QPKDFLSGTC LYLSSLSKKN
     PEALVPTSEP YVTGGNVLVD PTAKISPQAK IGPNVVIGPG AVIGEGARLS RCVVLANSTI
     KPHAFVKNSI IGWNGRVGRW ARIENVSVFG DDVEVKDEVY VNGGRVLPHK TISGNIEKPE
     IIM