ID R1C913_EMIHU Unreviewed; 819 AA.
AC R1C913;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=EMIHUDRAFT_102278 {ECO:0000313|EMBL:EOD18772.1};
OS Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD18772.1};
RN [1] {ECO:0000313|EMBL:EOD18772.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD18772.1};
RG DOE Joint Genome Institute;
RA Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT "Genome variability drives Emilianias global distribution.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000013827}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX PubMed=23760476; DOI=10.1038/nature12221;
RA Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA Wurch L.L.;
RT "Pan genome of the phytoplankton Emiliania underpins its global
RT distribution.";
RL Nature 499:209-213(2013).
RN [3] {ECO:0000313|EnsemblProtists:EOD18772}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
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DR EMBL; KB866393; EOD18772.1; -; Genomic_DNA.
DR RefSeq; XP_005771201.1; XM_005771144.1.
DR STRING; 2903.R1C913; -.
DR PaxDb; 2903-EOD18772; -.
DR EnsemblProtists; EOD18772; EOD18772; EMIHUDRAFT_102278.
DR GeneID; 17264303; -.
DR KEGG; ehx:EMIHUDRAFT_102278; -.
DR eggNOG; KOG2598; Eukaryota.
DR HOGENOM; CLU_018272_7_1_1; -.
DR OMA; YNIGSER; -.
DR Proteomes; UP000013827; Unassembled WGS sequence.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01169; HMPP_kinase; 1.
DR CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 3.
DR Pfam; PF02581; TMP-TENI; 3.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR SUPFAM; SSF51391; Thiamin phosphate synthase; 2.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000013827};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT DOMAIN 29..110
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 140..220
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 292..343
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 388..480
FT /note="Thiamine phosphate synthase/TenI"
FT /evidence="ECO:0000259|Pfam:PF02581"
FT DOMAIN 490..551
FT /note="Thiamine phosphate synthase/TenI"
FT /evidence="ECO:0000259|Pfam:PF02581"
FT DOMAIN 568..618
FT /note="Thiamine phosphate synthase/TenI"
FT /evidence="ECO:0000259|Pfam:PF02581"
FT REGION 249..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 82715 MW; E557FB6EA391D6F5 CRC64;
MYALLSLPAI VGTSADVGRP IVWSIAGSDS GGGAGVQADL LTCHSLGAHG CTVVTALTAQ
NSVGVRHVEL ASGDSVRATL HALAADLPPR AIKIGMLGGE ASVLEVGAFL AAAEAATEEA
GGAEGAAAGA YAARPFAASP SVVCDPVLVS SSGARLLSEE GLAALRSSVL PRCRLLTPNL
AEAEALLERR ITTAAEAEAA AVELRRRAGC GAVLLKGGHA AYFAAQGEGA AGGGRSPPPA
MDVLVDGGAP PVWRERSPQR RAARRLDAGG RARSLPNRLS CARVGATEAA GGGCHGTGCV
LSTAIAAMLA HGHPLVDSVV LAKAYVTQGM ASAAAVGAGP APVAHTGWPS SPSSMPVLSR
SAAAAAAPPR FARCDGDAAR GLYPVLDSKE SVAAAVAAGA RDVQLRIKGA GAARVASEVR
GAQAACAAAG ARLWVNDYGR IAVSEGAYGV HLGREGALAE AAPRASPKAL TRGVAARRRR
QEDLAALTDS EAGMEELRAL SDAGVRLGVS THTFAELAAA LAVGPSYVAL GPVFATTSKR
VVAAAAGPAA AGPAAAGPAV AAGEAPSREV EPKGLAGVAH WRALLPGDVP LVAIGGISLD
AAPSVLGAGA QGLAVIGALT GAPDLGAADG QMELGVRDGR AVISLQHDGV VIVPLPRDHG
NEEELRRDLQ RVSSAALGYD QPVEIKPMTD GADPNPVRGD SGEAAVEMSD GEVLMTADTT
RLSRYNDEVA AAYRTTVAFE EMMRNRAPGR APQRPTLILA TDTSTEVLAA LKRLVNGYSV
SPAKLIMDDD DDQSVDMDEL VFRPNPVERL ELSHSDDEE
//
