ID   L0AWH9_THEEQ            Unreviewed;       419 AA.
AC   L0AWH9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   ORFNames=BEWA_024620 {ECO:0000313|EMBL:AFZ79613.1};
OS   Theileria equi strain WA.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=1537102 {ECO:0000313|EMBL:AFZ79613.1, ECO:0000313|Proteomes:UP000031512};
RN   [1] {ECO:0000313|EMBL:AFZ79613.1, ECO:0000313|Proteomes:UP000031512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA {ECO:0000313|EMBL:AFZ79613.1,
RC   ECO:0000313|Proteomes:UP000031512};
RX   PubMed=23137308; DOI=10.1186/1471-2164-13-603;
RA   Kappmeyer L.S., Thiagarajan M., Herndon D.R., Ramsay J.D., Caler E.,
RA   Djikeng A., Gillespie J.J., Lau A.O., Roalson E.H., Silva J.C., Silva M.G.,
RA   Suarez C.E., Ueti M.W., Nene V.M., Mealey R.H., Knowles D.P., Brayton K.A.;
RT   "Comparative genomic analysis and phylogenetic position of Theileria
RT   equi.";
RL   BMC Genomics 13:603-603(2012).
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; CP001669; AFZ79613.1; -; Genomic_DNA.
DR   RefSeq; XP_004829279.1; XM_004829222.1.
DR   AlphaFoldDB; L0AWH9; -.
DR   STRING; 1537102.L0AWH9; -.
DR   EnsemblProtists; AFZ79613; AFZ79613; BEWA_024620.
DR   GeneID; 15807202; -.
DR   KEGG; beq:BEWA_024620; -.
DR   VEuPathDB; PiroplasmaDB:BEWA_024620; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   OrthoDB; 5486038at2759; -.
DR   UniPathway; UPA00126; UER00930.
DR   Proteomes; UP000031512; Chromosome 1.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR22572:SF15; MANNOSE-1-PHOSPHATE GUANYLTRANSFERASE BETA; 1.
DR   PANTHER; PTHR22572; SUGAR-1-PHOSPHATE GUANYL TRANSFERASE; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:AFZ79613.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031512};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFZ79613.1}.
FT   DOMAIN          3..234
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   419 AA;  45960 MW;  6F7F3948EC27AF2F CRC64;
     MKCVILAGGH GTRLRPLTLS VPKPLIEFCN RSIIEYQIDA AKKAGVDHII LAVSESQPAL
     AQRVQKLQEK YSIRIDCSIE TSPMGTAGPL RLAEKLICEP NDDSDDFLVL NSDVICDYPL
     LELLNSHRSK KATITILVTK VENPSEFGVI FHDEEFRIKS FVEKPTNYVS NQINAGVYVL
     SKTVVNSIPL ENTSIERDIF PKFVMLGNTF CHPLSGYWAD IGKPIEYLRG QHLYLSNNFS
     GDFNVCGTTE TCVSETEKRE ICEIDTGILI RTRSNANLED ADYVKSACAS TPRSDLLEAP
     TIYNNVNFKA PVLVHPTAKI GPGSLIGPNV CIGANVVIGK GSRIVRSTIM EGANVSPNSY
     IEGSIIGWNS RIGPWVRIEG LSVLGESVGI SEALFIRGCI VLPHKNVNNN IYEPGVIII
//