ID C0NJR8_AJECG Unreviewed; 374 AA.
AC C0NJR8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000256|ARBA:ARBA00018601};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
DE AltName: Full=GDP-mannose pyrophosphorylase {ECO:0000256|ARBA:ARBA00031190};
DE AltName: Full=GTP-mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00030179};
GN ORFNames=HCBG_03398 {ECO:0000313|EMBL:EEH08109.1};
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH08109.1, ECO:0000313|Proteomes:UP000001631};
RN [1] {ECO:0000313|Proteomes:UP000001631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC {ECO:0000313|Proteomes:UP000001631};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in cell wall synthesis where it is required for
CC glycosylation. Involved in cell cycle progression through cell-size
CC checkpoint. {ECO:0000256|ARBA:ARBA00024813}.
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:0000256|ARBA:ARBA00001083};
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. {ECO:0000256|ARBA:ARBA00004823}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000256|ARBA:ARBA00007274}.
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DR EMBL; GG663366; EEH08109.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NJR8; -.
DR STRING; 447093.C0NJR8; -.
DR VEuPathDB; FungiDB:I7I50_06998; -.
DR HOGENOM; CLU_029499_0_0_1; -.
DR InParanoid; C0NJR8; -.
DR OrthoDB; 5486038at2759; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000001631; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
DR CDD; cd05824; LbH_M1P_guanylylT_C; 1.
DR CDD; cd06425; M1P_guanylylT_B_like_N; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR045233; GMPPB_N.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22572:SF15; MANNOSE-1-PHOSPHATE GUANYLTRANSFERASE BETA; 1.
DR PANTHER; PTHR22572; SUGAR-1-PHOSPHATE GUANYL TRANSFERASE; 1.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:EEH08109.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001631};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..233
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 374 AA; 41272 MW; CE2B3897E7E8B23C CRC64;
MKALILVGGF GTRLRPLTLT LPKPLVEFAN RPMILHQVES LAAAGVTDIV LAVNYRPDVM
VSALKKYEEI YNVKIEFSVE SEPLGTAGPL KLAEKILGKD DSPFFVLNSD VICEYPFAEL
AAFHKKHGDE GTIVVTKVEE PSKYGVVVHK PNHPSRIDRF VEKPVEFVGN RINAGIYILN
PSVLNRIELR PTSIEQETFP AICKDGQLHS FDLEGFWMDV GQPKDFLTGT CLYLSSLTKR
ESKVLSPLSE PYVYGGNVLV DPSATIGKNC RIGPNVVIGP NVVVGDGVRL QRCVLLENSK
VKDHAWVKST IVGWNSAVGR WARLENVTVL GDDVTIGDEV YVNGGSILPH KSIKQNVDER
SNTSTTKKQE HIFL
//
