ID   MPG1_PICAN              Reviewed;         364 AA.
AC   Q9P8N0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=OPU24;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=11255248; DOI=10.1002/yea.678;
RA   Agaphonov M.O., Packeiser A.N., Chechenova M.B., Choi E.-S.,
RA   Ter-Avanesyan M.D.;
RT   "Mutation of the homologue of GDP-mannose pyrophosphorylase alters cell
RT   wall structure, protein glycosylation and secretion in Hansenula
RT   polymorpha.";
RL   Yeast 18:391-402(2001).
CC   -!- FUNCTION: Involved in cell wall synthesis where it is required for
CC       glycosylation. Involved in cell cycle progression through cell-size
CC       checkpoint. {ECO:0000269|PubMed:11255248}.
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}.
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; AF234177; AAF60300.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P8N0; -.
DR   SMR; Q9P8N0; -.
DR   PhylomeDB; Q9P8N0; -.
DR   UniPathway; UPA00126; UER00930.
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:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..364
FT                   /note="Mannose-1-phosphate guanyltransferase"
FT                   /id="PRO_0000238492"
SQ   SEQUENCE   364 AA;  40065 MW;  1700BCA9AF0308FD CRC64;
     MKGLILVGGY GTRLRPLTLS LPKPLVEFGN RPMILHQIEA LANAGCTDIV LAVNYKPEVM
     VGALKQYEKE YGVSITFSVE EEPLGTAGPL KLAEKILKKD NTPIFVLNSD VICEYPLRDL
     LEFHTAHGGE ATIVATKVDE PSKYGVIVHD RDVPNLIERF VEKPVEFVGN RINAGIYVLN
     PSVIDLIEMR PTSIEHETFP ILVEQKKLYS FDLPGYWMDV GQPKDFLSGM CLYLSALTKK
     NSNLLTSTSE EYVNGGNVLI DPSAKIGKGC KIGPNVVIGP NCIIGDGVRI QRSTILKNSQ
     IKDHAWVKST IVGWNSTVGK WARLEGVTVL GEDVTVKDEV YVNGGKVLPH KSIKDNVETP
     QIIM