MPG1_CANAL
ID MPG1_CANAL Reviewed; 362 AA.
AC O93827; A0A1D8PKY0; Q59MI2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Mannose-1-phosphate guanyltransferase;
DE EC=2.7.7.13;
DE AltName: Full=ATP-mannose-1-phosphate guanylyltransferase;
DE AltName: Full=CASRB1;
DE AltName: Full=GDP-mannose pyrophosphorylase;
GN Name=MPG1; Synonyms=SRB1, VIG9; OrderedLocusNames=CAALFM_C307950CA;
GN ORFNames=CaO19.6190;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1161;
RX PubMed=9782489; DOI=10.1099/00221287-144-9-2417;
RA Warit S., Walmsley R.M., Stateva L.I.;
RT "Cloning and sequencing of the Candida albicans homologue of
RT SRB1/PSA1/VIG9, the essential gene encoding GDP-mannose pyrophosphorylase
RT in Saccharomyces cerevisiae.";
RL Microbiology 144:2417-2426(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060;
RX PubMed=10913825; DOI=10.1016/s0304-4165(00)00075-1;
RA Ohta A., Chibana H., Arisawa M., Sudoh M.;
RT "The VIG9 gene products from the human pathogenic fungi Candida albicans
RT and Candida glabrata encode GDP-mannose pyrophosphorylase.";
RL Biochim. Biophys. Acta 1475:265-272(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 Evidence={ECO:0000269|PubMed:10913825};
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; AF030299; AAC64911.1; -; Genomic_DNA.
DR EMBL; AF030300; AAC64912.1; -; Genomic_DNA.
DR EMBL; AB020596; BAA34807.1; -; Genomic_DNA.
DR EMBL; CP017625; AOW28792.1; -; Genomic_DNA.
DR RefSeq; XP_710946.1; XM_705854.1.
DR AlphaFoldDB; O93827; -.
DR SMR; O93827; -.
DR BioGRID; 1230547; 3.
DR STRING; 237561.O93827; -.
DR COMPLUYEAST-2DPAGE; O93827; -.
DR PRIDE; O93827; -.
DR GeneID; 3647454; -.
DR KEGG; cal:CAALFM_C307950CA; -.
DR CGD; CAL0000178573; SRB1.
DR VEuPathDB; FungiDB:C3_07950C_A; -.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_0_0_1; -.
DR InParanoid; O93827; -.
DR OMA; PFLTHQL; -.
DR OrthoDB; 806744at2759; -.
DR BRENDA; 2.7.7.13; 1096.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IDA:CGD.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IGI:CGD.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IDA:CGD.
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; 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 1: Evidence at protein level;
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_0000068739"
FT VARIANT 197..198
FT /note="ET -> DP (in strain: 1161)"
FT VARIANT 333
FT /note="E -> Q (in strain: 1161)"
FT CONFLICT 289
FT /note="Q -> R (in Ref. 1; AAC64912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 39975 MW; 052DCC32D0E16923 CRC64;
MKGLILVGGY GTRLRPLTLT LPKPLVEFGN RPMILHQIEA LAAAGVTDIV LAVNYRPEVM
VSTLKKYEEE YGVSITFSVE EEPLGTAGPL KLAEEVLKKD DSPFFVLNSD VICDYPFKEL
ADFHKAHGAA GTIVATKVDE PSKYGVIVHD RDTPNLIDRF VEKPVEFVGN RINAGLYILN
PSVIDLIEMR PTSIEKETFP ILVEQKQLYS FDLEGYWMDV GQPKDFLSGT CLYLTSLSKK
HPEKLCKEKY VHGGNVLIDP TAKIHPSALI GPNVTIGPNV VVGEGARIQR SVLLANSQVK
DHAWVKSTIV GWNSRIGKWA RTEGVTVLGD DVEVKNEIYV NGAKVLPHKS ISSNVEKESI
IM
