ID A0A1Z5TL76_HORWE Unreviewed; 364 AA.
AC A0A1Z5TL76;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=BTJ68_03283 {ECO:0000313|EMBL:OTA36725.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA36725.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA36725.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA36725.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OTA36725.1}.
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DR EMBL; MUNK01000028; OTA36725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5TL76; -.
DR STRING; 1157616.A0A1Z5TL76; -.
DR VEuPathDB; FungiDB:BTJ68_03283; -.
DR InParanoid; A0A1Z5TL76; -.
DR OrthoDB; 5486038at2759; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000194280; 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OTA36725.1}.
FT DOMAIN 2..233
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 364 AA; 39954 MW; 1D3E42DE5D2C1F0F CRC64;
MKALILVGGF GTRLRPLTLT LPKPLVEFGN RPMILHQVEA LAAAGVTDIV LAVNYRPEIM
TAALKKYEQE YNVNIEFSVE TEPLGTAGPL KLAEKILGKD DSPFFVLNSD IICDYPFGDL
AKFHKNHGNE GTIVVTKVEE PSKYGVVVHK PDHPSRIDRF VEKPVEFVGN RINAGIYILN
PSVLKRIELR PTSIEQETFP AIVKEGQLHS YDLEGFWMDV GQPKDFLSGT CLYLSSLAQK
KSNLLTSTSE PYVHGGNVMI DPSATIGKNC KIGPNVTIGP NVVIGDGVRL QRCVLLQGSK
VKEHAWIKST IVGWNSTVGR WARLENVSVL GDDVTIGDEI YCNGASVLPH KSIKQNVDAP
SIIM
//
