ID   GMPPB_PIG               Reviewed;         360 AA.
AC   P0C5I2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Mannose-1-phosphate guanyltransferase beta;
DE            EC=2.7.7.13 {ECO:0000269|PubMed:11082198};
DE   AltName: Full=GDP-mannose pyrophosphorylase 37-kDa subunit;
DE   AltName: Full=GDP-mannose pyrophosphorylase B;
DE   AltName: Full=GTP-mannose-1-phosphate guanylyltransferase beta;
GN   Name=GMPPB {ECO:0000250|UniProtKB:Q9Y5P6};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-23; 159-170 AND 180-194,
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=11082198; DOI=10.1046/j.1432-1033.2000.01781.x;
RA   Ning B., Elbein A.D.;
RT   "Cloning, expression and characterization of the pig liver GDP-mannose
RT   pyrophosphorylase. Evidence that GDP-mannose and GDP-Glc pyrophosphorylases
RT   are different proteins.";
RL   Eur. J. Biochem. 267:6866-6874(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-23, AND INTERACTION WITH GMPPA.
RX   PubMed=7688733; DOI=10.1016/s0021-9258(17)46796-2;
RA   Szumilo T., Drake R.R., York J.L., Elbein A.D.;
RT   "GDP-mannose pyrophosphorylase. Purification to homogeneity, properties,
RT   and utilization to prepare photoaffinity analogs.";
RL   J. Biol. Chem. 268:17943-17950(1993).
CC   -!- FUNCTION: Catalyzes the formation of GDP-mannose, an essential
CC       precursor of glycan moieties of glycoproteins and glycolipids.
CC       {ECO:0000269|PubMed:11082198}.
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:0000269|PubMed:11082198};
CC   -!- ACTIVITY REGULATION: Activated by Mn(2+).
CC       {ECO:0000269|PubMed:11082198}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.2 mM for mannose-1-phosphate {ECO:0000269|PubMed:11082198};
CC         KM=0.36 mM for GTP {ECO:0000269|PubMed:11082198};
CC         KM=39 nM for GDP-mannose {ECO:0000269|PubMed:11082198};
CC         Vmax=0.56 mmol/min/mg enzyme toward mannose-1-phosphate
CC         {ECO:0000269|PubMed:11082198};
CC         Vmax=14 nmol/min/mg enzyme toward GDP-mannose
CC         {ECO:0000269|PubMed:11082198};
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:0000269|PubMed:11082198}.
CC   -!- SUBUNIT: Associates with GMPPA (in vivo). {ECO:0000269|PubMed:7688733}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y5P6}.
CC   -!- TISSUE SPECIFICITY: Expressed in the liver (at protein level).
CC       {ECO:0000269|PubMed:11082198}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0C5I2; -.
DR   SMR; P0C5I2; -.
DR   STRING; 9823.ENSSSCP00000012142; -.
DR   PaxDb; P0C5I2; -.
DR   PeptideAtlas; P0C5I2; -.
DR   PRIDE; P0C5I2; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   InParanoid; P0C5I2; -.
DR   SABIO-RK; P0C5I2; -.
DR   UniPathway; UPA00126; UER00930.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IDA:MGI.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; GTP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..360
FT                   /note="Mannose-1-phosphate guanyltransferase beta"
FT                   /id="PRO_0000307164"
SQ   SEQUENCE   360 AA;  39827 MW;  723579381B292BB4 CRC64;
     MKALILVGGY GTRLRPLTLS IPKPLVDFCN KPILLHQVEA LASAGVDHVI LAVSYMSQML
     EKEMKAQEQR LGIRISMSHE EEPLGTAGPL ALARDLLSET AEPFFVLNSD VICDFPFQAM
     VQFHRHHGQE GSILVTKVEE PSKYGVVVCE ADTGRIHRFV EKPQVFVSNK INAGMYILSP
     AVLQRIQLQP TSIEKEIFPV MAKEGQLYAM ELQGFWMDIG QPKDFLTGMC LFLQSLRQKQ
     PEQLCSGPGI VGNVLVDPSA RIGKNCSIGP NVSLGPGVVV EDGVCIRRCT VLRDARIRSH
     SWLESCIVCW RCRVGQWVRM ENVTVLGEDV IVNDELYLNG ASVLPHKSIG ESVPEPGIIM