ID   A3GHU9_PICST            Unreviewed;       461 AA.
AC   A3GHU9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   04-NOV-2026, entry version 76.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   Name=MPG2 {ECO:0000313|EMBL:EAZ63117.1};
GN   ORFNames=PICST_53940 {ECO:0000313|EMBL:EAZ63117.1};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:EAZ63117.1, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:EAZ63117.1, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = GDP-alpha-D-mannose
CC         + diphosphate; 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:0000256|ARBA:ARBA00047343};
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. {ECO:0000256|ARBA:ARBA00004823}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000256|ARBA:ARBA00007274}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAZ63117.1}.
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DR   EMBL; AAVQ01000002; EAZ63117.1; -; Genomic_DNA.
DR   STRING; 322104.A3GHU9; -.
DR   KEGG; pic:PICST_53940; -.
DR   eggNOG; KOG1460; Eukaryota.
DR   HOGENOM; CLU_029499_3_0_1; -.
DR   InParanoid; A3GHU9; -.
DR   OMA; AAAMVMW; -.
DR   OrthoDB; 285674at2759; -.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   InterPro; IPR056729; GMPPB_C.
DR   InterPro; IPR050486; Mannose-1P_guanyltransferase.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22572; SUGAR-1-PHOSPHATE GUANYL TRANSFERASE; 1.
DR   Pfam; PF25087; GMPPB_C; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR   Proteomes; UP000002258; Chromosome 1.
DR   AlphaFoldDB; A3GHU9; -.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase {ECO:0000313|EMBL:EAZ63117.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW   Transferase {ECO:0000313|EMBL:EAZ63117.1}.
FT   DOMAIN          4..149
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          343..456
FT                   /note="Mannose-1-phosphate guanyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF25087"
SQ   SEQUENCE   461 AA;  51855 MW;  12526BE68D2518BB CRC64;
     MTIKAVILVG GETTGTRFRP LSMESPKVLF PICGKPLVSH VIDNLVSQLS STEPLEILLI
     GFFKDSSKFD DYIKIKNKQY PDVKIKYLSE PNSMGTAGGL YYFREEIFGD ETCEKLLVIH
     GDVICNYPFK QLLDFYDAEN SSAVILGIDP VLLMNNFHNK KQIQNQDQSS FVTYDKDRIF
     SLYGTIIAKK ANNEVVHYVE KPTSKISKFR METDYNVLLN GGIYVFNRNV LSELETAHVR
     HKDPSTYFEF HDDLEEDNVD DKSISLELDI LRTLPTTPNT KFSTYKSNSF WYQLKTPVSA
     LMANNFFLEQ LLQNDQYKTL EPPSAGVVPP VLSVGSCLQN TATYKIGPNV SIGKNVTIGR
     GVRIINSIIS NNVTIGDNTF ISNSIVSDGV KIGKWCRIEG TITSTTISND NASNSDGYFK
     LINNIVILCQ NTVVNNQVFV YNSIVLPHKE LKSDVKYEIV M
//