ID U4KWT3_PYROM Unreviewed; 531 AA.
AC U4KWT3;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Similar to Probable thiamine biosynthetic bifunctional enzyme acc. no. P40386 {ECO:0000313|EMBL:CCX06106.1};
GN ORFNames=PCON_05693 {ECO:0000313|EMBL:CCX06106.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX06106.1};
RN [1] {ECO:0000313|EMBL:CCX06106.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX06106.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX06106.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-
CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate
CC + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575,
CC ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000876};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl
CC phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2
CC H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001829};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl-
CC 5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine
CC phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58296; EC=2.5.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001159};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-
CC phosphooxyethyl)-thiazole + ADP + H(+); Xref=Rhea:RHEA:24212,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17957, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58296, ChEBI:CHEBI:456216; EC=2.7.1.50;
CC Evidence={ECO:0000256|ARBA:ARBA00001771};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-
CC methylthiazole: step 1/1. {ECO:0000256|ARBA:ARBA00004868}.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine
CC and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005165}.
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DR EMBL; HF935280; CCX06106.1; -; Genomic_DNA.
DR AlphaFoldDB; U4KWT3; -.
DR STRING; 1076935.U4KWT3; -.
DR eggNOG; ENOG502QS2M; Eukaryota.
DR OMA; GQTDMPI; -.
DR OrthoDB; 2784451at2759; -.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000018144; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01170; THZ_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 HAMAP; MF_00228; Thz_kinase; 1.
DR HAMAP; MF_00097; TMP_synthase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000417; Hyethyz_kinase.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR InterPro; IPR034291; TMP_synthase.
DR NCBIfam; TIGR00693; thiE; 1.
DR NCBIfam; TIGR00694; thiM; 1.
DR PANTHER; PTHR20857:SF15; THIAMINE BIOSYNTHETIC BIFUNCTIONAL ENZYME; 1.
DR PANTHER; PTHR20857; THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; 1.
DR Pfam; PF02110; HK; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR PRINTS; PR01099; HYETHTZKNASE.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..212
FT /note="Thiamine phosphate synthase/TenI"
FT /evidence="ECO:0000259|Pfam:PF02581"
SQ SEQUENCE 531 AA; 56750 MW; 4AEF597F9754F48E CRC64;
MPKPSLDLTL YLVTNSELLP AGRTLVQHVE EAIRGGVTIV QLREKTMATR AFISLGRELH
NVTQKYGVPL LINDRIDVAL AVGCEGVHIG WEDAEYADAR RLLGNDKIIG VSVSNNDQAE
EAAATGCDYI GVGPVFATST KPNHNPALGT PGLRNLLEFI STLPGPTGNW GLKVPSVAIG
GINLDNVQRV MYQSESLGRK KSLSGVAVVS AIIASLTPED VCKSFVKLLE YCENPVFAPW
QLQIANASDF NDLFKKIATK VATKKPIVHH VTNNVVKNFS ANVTLAVGAS PIMSEDLSEL
PELAAFNGAM VLNMGTSTKA QQGFLLAAAK ASNAAGNPVV FDPVGAGATS LRRESTALIV
GNAYCDIIKG NESEIRTVLG DDVIQQRGVD STSTTDDPLE KARLVKQLAR RERNIIVMTG
KVDYVSDGES TFELSDGHEI QGGVTGTGCS LGSIIAAYVS IHRECKLVAV LAAISAYNAA
AREAAEGVKI LGPGAWMTAF LDRLYELRTA DKVEEETWVR KLGERVKLVD V
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