ID   GMPPA_XENTR             Reviewed;         421 AA.
AC   Q0VFM6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Mannose-1-phosphate guanyltransferase alpha;
DE   AltName: Full=GDP-mannose pyrophosphorylase A;
DE   AltName: Full=GTP-mannose-1-phosphate guanylyltransferase alpha;
GN   Name=gmppa;
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=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May serve as a regulatory subunit and allow allosteric
CC       feedback inhibition of GMPPB by GDP-mannose. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
CC   -!- CAUTION: GMPPA is a close homolog of GMPPB, that has been shown to
CC       catalyze the formation of GDP-mannose, an essential precursor of glycan
CC       moieties of glycoproteins and glycolipids. It has been hypothesized
CC       that GMPPA might serve as a regulatory subunit and allow allosteric
CC       feedback inhibition of GMPPB by GDP-mannose. Alignment of GMPPAs and
CC       GMPPBs from various species shows that GMPPAs are characterized by a 2
CC       amino acid-insertion (residues 11-12) in a highly conserved motif that
CC       borders the catalytic pocket and binds the nucleotide substrate in
CC       homologous enzymes. This insertion might inactivate the ancestral
CC       catalytic site, converting it to an allosteric site. {ECO:0000305}.
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DR   EMBL; BC118773; AAI18774.1; -; mRNA.
DR   RefSeq; NP_001072208.1; NM_001078740.1.
DR   RefSeq; XP_012825984.1; XM_012970530.2.
DR   AlphaFoldDB; Q0VFM6; -.
DR   SMR; Q0VFM6; -.
DR   STRING; 8364.ENSXETP00000041698; -.
DR   PaxDb; Q0VFM6; -.
DR   DNASU; 779654; -.
DR   GeneID; 779654; -.
DR   KEGG; xtr:779654; -.
DR   CTD; 29926; -.
DR   eggNOG; KOG1460; Eukaryota.
DR   HOGENOM; CLU_029499_3_0_1; -.
DR   InParanoid; Q0VFM6; -.
DR   OrthoDB; 806744at2759; -.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000019242; Expressed in neurula embryo and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.90.550.10; -; 1.
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   Cytoplasm; Reference proteome.
FT   CHAIN           1..421
FT                   /note="Mannose-1-phosphate guanyltransferase alpha"
FT                   /id="PRO_0000327880"
SQ   SEQUENCE   421 AA;  46232 MW;  6ADD7947E4F48F7B CRC64;
     MLKAVILIGG PQKGTRFRPL SFEVPKPLFP VAGVPMVQHH IEACSKVPNL KEILLIGFYQ
     PNEALSSFLL KAQQEFKVAI RYLQEYSALG TGGGIYHFRD QILSGGPQAF FVMNADVCSA
     FPLVPMLDFH KQHGGSQSYV ILGTTANRSQ SLNYGCIVAN GETQEVLHYV EKPGTFVSDI
     INCGIYLFSP SIFQHIAEVF QRNQQELQLE ENSSWQRTEV IRLEQDVFTT LAGRGKLYVY
     KTEGCWSQIK SAGSAIYASR LYLSQYGSTH PERLASTKEG GPTIRGNVYI HPTANVDPSA
     VLGPNVSIGM GVTVGAGVRI RESIVLHGAV LQDHSCVLNT IVGWDSTVGR WARVEGTPSD
     PNPNDPYSKI DSETLFREGK LTPSITILGC NVSIPAEVVI LNSIVLPHKE LSRSFKNQII
     L