GMPPA_PAPAN
ID GMPPA_PAPAN Reviewed; 420 AA.
AC B0CM52;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA Tsipouri V., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (JAN-2008) 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 -!- SUBUNIT: Associates with GMPPB. {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; DP000550; ABY67209.1; -; Genomic_DNA.
DR RefSeq; NP_001162569.1; NM_001169098.1.
DR RefSeq; XP_009181414.1; XM_009183150.1.
DR RefSeq; XP_009181415.1; XM_009183151.2.
DR RefSeq; XP_009181416.1; XM_009183152.1.
DR AlphaFoldDB; B0CM52; -.
DR SMR; B0CM52; -.
DR STRING; 9555.ENSPANP00000017912; -.
DR Ensembl; ENSPANT00000080991; ENSPANP00000047838; ENSPANG00000018458.
DR GeneID; 100137607; -.
DR KEGG; panu:100137607; -.
DR CTD; 29926; -.
DR eggNOG; KOG1460; Eukaryota.
DR GeneTree; ENSGT00940000157018; -.
DR HOGENOM; CLU_029499_3_0_1; -.
DR OMA; MPVPNWW; -.
DR OrthoDB; 806744at2759; -.
DR Proteomes; UP000028761; Chromosome 10.
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 3: Inferred from homology;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..420
FT /note="Mannose-1-phosphate guanyltransferase alpha"
FT /id="PRO_0000327874"
SQ SEQUENCE 420 AA; 46288 MW; 72BC24BC15C9C9A1 CRC64;
MLKAVILIGG PQKGTRFRPL SFEVPKPLFP VAGVPMIQHH IEACAQVPGM QEILLIGFYQ
PDEPLTQFLE AAQQEFNLPV RYLQEFAPLG TGGGLYHFRD QILAGSPEAF FVLNADVCSD
FPLSAMLEAH RRQRHPFLLL GTTANRTQSL NYGCIVENPQ THEVLHYVEK PSTFISDIIN
CGIYLFSPEA LKPLRDVFQR NQQDGQLEDS PGLWPGAGTI RLEQDVFSAL AGQGQIYVHL
TDGIWSQIKS AGSALYASRL YLSRYQDTHP ERLAKHTPGG PRIRGNVYIH PTAKVAPSAV
LGPNVSIGKG VTVGEGVRLR ESIVLHGATL QEHTCVLHSI VGWGSTVGRW ARVEGTPNDP
NPNDPRARMD SESLFKDGKL LPAITILGCR VRIPAEVLIL NSIVLPHKEL SRSFTNQIIL