ID   GMPPB_XENTR             Reviewed;         360 AA.
AC   Q68EQ1;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Mannose-1-phosphate guanyltransferase beta;
DE            EC=2.7.7.13 {ECO:0000250|UniProtKB:P0C5I2};
DE   AltName: Full=GDP-mannose pyrophosphorylase B;
DE   AltName: Full=GTP-mannose-1-phosphate guanylyltransferase beta;
GN   Name=gmppb; ORFNames=TGas135o02.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of GDP-mannose, an essential
CC       precursor of glycan moieties of glycoproteins and glycolipids.
CC       {ECO:0000250|UniProtKB:P0C5I2}.
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:0000250|UniProtKB:P0C5I2};
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:0000250|UniProtKB:P0C5I2}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
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DR   EMBL; CR760719; CAJ83390.1; -; mRNA.
DR   EMBL; BC080150; AAH80150.1; -; mRNA.
DR   RefSeq; NP_001008434.1; NM_001008434.2.
DR   RefSeq; XP_012820014.1; XM_012964560.2.
DR   AlphaFoldDB; Q68EQ1; -.
DR   SMR; Q68EQ1; -.
DR   STRING; 8364.ENSXETP00000013087; -.
DR   PaxDb; Q68EQ1; -.
DR   GeneID; 493267; -.
DR   KEGG; xtr:493267; -.
DR   CTD; 29925; -.
DR   Xenbase; XB-GENE-922650; gmppb.
DR   eggNOG; KOG1322; Eukaryota.
DR   HOGENOM; CLU_029499_0_0_1; -.
DR   InParanoid; Q68EQ1; -.
DR   OMA; EWMDCGN; -.
DR   OrthoDB; 806744at2759; -.
DR   TreeFam; TF300718; -.
DR   UniPathway; UPA00126; UER00930.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
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:0009298; P:GDP-mannose biosynthetic process; ISS:UniProtKB.
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   GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..360
FT                   /note="Mannose-1-phosphate guanyltransferase beta"
FT                   /id="PRO_0000307168"
SQ   SEQUENCE   360 AA;  40161 MW;  AE6206C213A961C8 CRC64;
     MKALILVGGY GTRLRPLTLS VPKPLVDFCN KPILLHQVEA LVKAGVNHVI LAVSYMSDML
     EKEMKEQEKR LGIRISMSHE KEPLGTAGPL ALARELLTEN SDPFFVLNSD VICDFPFEEM
     VRFHKHHGKE GTIVVTKVEE PSKYGVVVYE AESGQIQRFV EKPQVFVSNK INSGLYIFSP
     AVLDRIQLRP TSIEKEIFPA MAQEGQLFAM ELQGFWMDIG QPKDFLTGMC MYLQSVRQKH
     PEWLHVGPGF IGNVLVDPTA KIGQNCSIGP NVTIGPGVTV EDGVRIKRCT IMKGSRLHSH
     SWLESSIVGW SSSVGQWVRM ENVTVLGEDV IVNDELYLNG ANVLPHKCIS ESVPEPRIIM