ID J8Q1C8_SACAR Unreviewed; 540 AA. AC J8Q1C8; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 13-SEP-2023, entry version 35. DE SubName: Full=Thi6p {ECO:0000313|EMBL:EJS41454.1}; GN ORFNames=SU7_3478 {ECO:0000313|EMBL:EJS41454.1}; OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS41454.1, ECO:0000313|Proteomes:UP000006968}; RN [1] {ECO:0000313|EMBL:EJS41454.1, ECO:0000313|Proteomes:UP000006968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H-6 / AS 2.3317 / CBS 10644 RC {ECO:0000313|Proteomes:UP000006968}; RX PubMed=23368932; DOI=10.1186/1471-2164-14-69; RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A., RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N., RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.; RT "High quality de novo sequencing and assembly of the Saccharomyces RT arboricolus genome."; RL BMC Genomics 14:69-69(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}. 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:EJS41454.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ALIE01000192; EJS41454.1; -; Genomic_DNA. DR AlphaFoldDB; J8Q1C8; -. DR HOGENOM; CLU_019943_1_1_1; -. DR OrthoDB; 2784451at2759; -. DR UniPathway; UPA00060; UER00139. DR Proteomes; UP000006968; Chromosome XVI. 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_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:SF23; 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 Reference proteome {ECO:0000313|Proteomes:UP000006968}; KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 12..212 FT /note="Thiamine phosphate synthase/TenI" FT /evidence="ECO:0000259|Pfam:PF02581" SQ SEQUENCE 540 AA; 58014 MW; 9356D5D54193C060 CRC64; MVFAKEDVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDTE TKNFIEEALE VQKICKKYNV PLIINDRIDV AMAIDADGVH VGQEDMPIPM VRKLLGSSKI LGWSVGKRSE VETLAKWGPD MVDYVGVGTL FPTLTKKNPK KTPMGTQGAI SVLNALEEFK ATWCRTVGIG GIHPDNIQRV ICQCVSSNGK RSLDGISLVS DIMASTDACA ATQKLKTLIN GTKYQFVECK LDATLPTAAS IQKVLFQVSS NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL ARIPNASLLL NTGTVAPIGM LKAAINAYNE VNRPITFDPV GYSATETRFH LNNTLLTYGQ FACIKGNYSE ILSLAELNKD KMKGVDSSSG DTDINLVARA TQIVAFKYRT VAVCTGEIDC IADGTFGGEY KLSSGTAGVT AEDIPCVLIE DGPIPIMGDI TASGCSLGST IACFIGGLDP TGNLFDAVVG AVLLYKSAGK LASTHCQGSG SFHFQLIDAL YQLFHENKPE KWSASLKKFN //