MPG1_DEBHA
ID MPG1_DEBHA Reviewed; 362 AA.
AC Q6BN12;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Mannose-1-phosphate guanyltransferase;
DE EC=2.7.7.13;
DE AltName: Full=ATP-mannose-1-phosphate guanylyltransferase;
DE AltName: Full=GDP-mannose pyrophosphorylase;
GN Name=MPG1; OrderedLocusNames=DEHA2F01056g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Involved in cell wall synthesis where it is required for
CC glycosylation. Involved in cell cycle progression through cell-size
CC checkpoint (By similarity). {ECO:0000250}.
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 -!- 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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; CR382138; CAG88712.1; -; Genomic_DNA.
DR RefSeq; XP_460408.1; XM_460408.1.
DR AlphaFoldDB; Q6BN12; -.
DR SMR; Q6BN12; -.
DR STRING; 4959.XP_460408.1; -.
DR EnsemblFungi; CAG88712; CAG88712; DEHA2F01056g.
DR GeneID; 2903808; -.
DR KEGG; dha:DEHA2F01056g; -.
DR VEuPathDB; FungiDB:DEHA2F01056g; -.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_0_0_1; -.
DR InParanoid; Q6BN12; -.
DR OMA; PFLTHQL; -.
DR OrthoDB; 806744at2759; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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.
PE 3: Inferred from homology;
KW Cell cycle; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..362
FT /note="Mannose-1-phosphate guanyltransferase"
FT /id="PRO_0000238487"
SQ SEQUENCE 362 AA; 39898 MW; 263E31EF2BE34716 CRC64;
MKGLILVGGY GTRLRPLTLT LPKPLVEFGN RPMILHQIEA LAKAGVTDIV LAVNYRPEVM
VSTLKKYEAE YGVTITFSVE EEPLGTAGPL KLAEKVLKKD DTPIFVLNSD VICDYPFQEL
ADFHKTSGGK ATIVATKVDE PSKYGVIVHD RDTPNLIDRF VEKPVEFVGN RINAGLYILN
PSVIDLIEMK PTSIEKETFP ILVENKELYS FDLEGYWMDV GQPKDFLSGT VLYLTALSKK
EPKKLCNEKF IHGGNVLVDP SAKIHPSALI GPNVVIGPNV VVGEGARIQR SVLLSNSEVK
DHAWVKSTIV GWNSRIGKWA RTDGITVLGD DVEIKNEVYV NGAKVLPHKS ISSNVEHEAI
IM