ID   MPG1_SCHPO              Reviewed;         363 AA.
AC   O74484; P78779;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 145.
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; ORFNames=SPCC1906.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=16049679; DOI=10.1007/s00438-005-0005-8;
RA   Donoso I., Munoz-Centeno M.C., Sanchez-Duran M.A., Flores A., Daga R.R.,
RA   Guevara C.M., Bejarano E.R.;
RT   "Mpg1, a fission yeast protein required for proper septum structure, is
RT   involved in cell cycle progression through cell-size checkpoint.";
RL   Mol. Genet. Genomics 274:155-167(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Involved in cell wall synthesis where it is required for
CC       glycosylation. Involved in cell cycle progression through cell-size
CC       checkpoint. Required for the correct assembly of the septum.
CC       {ECO:0000269|PubMed:16049679}.
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:0000269|PubMed:16049679}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
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DR   EMBL; D89128; BAA13790.1; -; mRNA.
DR   EMBL; CU329672; CAA20770.1; -; Genomic_DNA.
DR   PIR; T41209; T41209.
DR   PIR; T42371; T42371.
DR   RefSeq; NP_588405.1; NM_001023396.2.
DR   AlphaFoldDB; O74484; -.
DR   SMR; O74484; -.
DR   BioGRID; 275326; 7.
DR   STRING; 4896.SPCC1906.01.1; -.
DR   iPTMnet; O74484; -.
DR   MaxQB; O74484; -.
DR   PaxDb; O74484; -.
DR   PRIDE; O74484; -.
DR   EnsemblFungi; SPCC1906.01.1; SPCC1906.01.1:pep; SPCC1906.01.
DR   PomBase; SPCC1906.01; mpg1.
DR   VEuPathDB; FungiDB:SPCC1906.01; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   HOGENOM; CLU_029499_0_0_1; -.
DR   InParanoid; O74484; -.
DR   OMA; PFLTHQL; -.
DR   PhylomeDB; O74484; -.
DR   UniPathway; UPA00126; UER00930.
DR   PRO; PR:O74484; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; ISO:PomBase.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
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; 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; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Septation; Transferase.
FT   CHAIN           1..363
FT                   /note="Mannose-1-phosphate guanyltransferase"
FT                   /id="PRO_0000068740"
FT   CONFLICT        175..176
FT                   /note="GI -> VL (in Ref. 2; BAA13790)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   363 AA;  39719 MW;  55F55FF0ED017C02 CRC64;
     MKALILVGGF GTRLRPLTLT LPKPLVEFGN KPMILHQVEA LAAAGVTDIV LAVNYRPEIM
     VEALKKYEKE YNVNITFSVE NEPLGTAGPL ALARDILAKD HSPFFVLNSD VICEYPFADL
     AAFHKAHGAE GTIVVTKVEE PSKYGVVVHY PNSESLIERF VEKPVEFVSN RINGGIYILN
     PSVLDRIEPR PTSIEKEVFP AMVNDKQLHS FDLEGYWMDV GQPKDYLTGT CLYLSSLRKH
     KPEILAPASS NIIGNVLIDP SATIGKNCKI GPNVVIGPNV TIGDGVRLQR CAILKSSRVR
     DHAWVKSSIV GWNSTLGSWS RLENVSVLGD DVVVNDEIYV NGGSILPHKS ISANIEVPGT
     IVM