MPG1_HYPJE
ID MPG1_HYPJE Reviewed; 364 AA.
AC O74624;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Mannose-1-phosphate guanyltransferase;
DE EC=2.7.7.13;
DE AltName: Full=GDP-mannose pyrophosphorylase;
DE AltName: Full=GTP-mannose-1-phosphate guanylyltransferase;
GN Name=mpg1;
OS Hypocrea jecorina (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=51453;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 56765 / Rut C-30;
RX PubMed=9644208; DOI=10.1007/s002940050358;
RA Kruszewska J.S., Saloheimo M., Penttila M., Palamarczyk G.;
RT "Isolation of a Trichoderma reesei cDNA encoding GTP: alpha-D-mannose-1-
RT phosphate guanyltransferase involved in early steps of protein
RT glycosylation.";
RL Curr. Genet. 33:445-450(1998).
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:9644208};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U89991; AAC39498.1; -; mRNA.
DR AlphaFoldDB; O74624; -.
DR SMR; O74624; -.
DR PRIDE; O74624; -.
DR VEuPathDB; FungiDB:TrQ_006497; -.
DR OMA; PFLTHQL; -.
DR BRENDA; 2.7.7.13; 6451.
DR UniPathway; UPA00126; UER00930.
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.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..364
FT /note="Mannose-1-phosphate guanyltransferase"
FT /id="PRO_0000238493"
SQ SEQUENCE 364 AA; 40285 MW; 66203BAF15284EBA CRC64;
MKGLILVGGF GTRLRPLTLT LPKPLVEFCN KPMIVHQIEA LVAAGVTDIV LAVNYRPEIM
EKFLAEYEEK YNINIEFSVE SEPLDTAGPL KLAERILGKD DSPFFVLNSD VICDYPFKEL
LEFHKAHGDE GTIVVTKVEE PSKYGVVVHK PNHPSRIDRF VEKPVEFVGN RINAGMYIFN
PSVLKRIELR PTSIEKETFP AMVADNQLHS FDLEGFWMDV GQPKDFLSGT CLYLSSLTKK
GSKELTPPTE PYVHGGNVMI HPSAKIGKNC RIGPNVTIGP DVVVGDGVRL QRCVLLKGSK
VKDHAWVKST IVGWNSTVGR WARLENVTVL GDDVTIGDEI YVNGGSVLPH KSIKANVDVP
AIIM