ID THI4_SOLM1 Reviewed; 263 AA. AC C4XIR5; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 28-JUN-2023, entry version 83. DE RecName: Full=Thiamine thiazole synthase {ECO:0000255|HAMAP-Rule:MF_00304}; DE EC=2.4.2.59 {ECO:0000255|HAMAP-Rule:MF_00304}; GN Name=thi4 {ECO:0000255|HAMAP-Rule:MF_00304}; OrderedLocusNames=DMR_31420; OS Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1) OS (Desulfovibrio magneticus). OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales; OC Desulfovibrionaceae; Solidesulfovibrio. OX NCBI_TaxID=573370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700980 / DSM 13731 / RS-1; RX PubMed=19675025; DOI=10.1101/gr.088906.108; RA Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N., RA Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H., RA Matsunaga T.; RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed RT common gene clusters in magnetotactic bacteria."; RL Genome Res. 19:1801-1808(2009). CC -!- FUNCTION: Involved in the biosynthesis of the thiazole moiety of CC thiamine. Catalyzes the conversion of NAD and glycine to adenosine CC diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an CC adenylated thiazole intermediate, using free sulfide as a source of CC sulfur. {ECO:0000255|HAMAP-Rule:MF_00304}. CC -!- CATALYTIC ACTIVITY: CC Reaction=glycine + hydrogen sulfide + NAD(+) = ADP-5-ethyl-4- CC methylthiazole-2-carboxylate + H(+) + 3 H2O + nicotinamide; CC Xref=Rhea:RHEA:55704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29919, ChEBI:CHEBI:57305, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:139151; EC=2.4.2.59; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00304}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00304}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00304}. CC -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000255|HAMAP- CC Rule:MF_00304}. CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP- CC Rule:MF_00304}. 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; AP010904; BAH76633.1; -; Genomic_DNA. DR RefSeq; WP_015861787.1; NC_012796.1. DR AlphaFoldDB; C4XIR5; -. DR SMR; C4XIR5; -. DR STRING; 573370.DMR_31420; -. DR EnsemblBacteria; BAH76633; BAH76633; DMR_31420. DR KEGG; dma:DMR_31420; -. DR eggNOG; COG1635; Bacteria. DR HOGENOM; CLU_053727_2_0_7; -. DR OMA; MWGGGMM; -. DR OrthoDB; 9777740at2; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000009071; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016763; F:pentosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0052837; P:thiazole biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR HAMAP; MF_00304; Thi4; 1. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR002922; Thi4_fam. DR InterPro; IPR022828; Thi4_prok. DR PANTHER; PTHR43422; THIAMINE THIAZOLE SYNTHASE; 1. DR PANTHER; PTHR43422:SF3; THIAMINE THIAZOLE SYNTHASE; 1. DR Pfam; PF01946; Thi4; 1. DR PRINTS; PR00420; RNGMNOXGNASE. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR TIGRFAMs; TIGR00292; thiazole biosynthesis enzyme; 1. PE 3: Inferred from homology; KW Iron; Metal-binding; NAD; Thiamine biosynthesis; Transferase. FT CHAIN 1..263 FT /note="Thiamine thiazole synthase" FT /id="PRO_1000205004" FT BINDING 36 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_note="ligand shared between two adjacent protomers" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304" FT BINDING 55..56 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_note="ligand shared between two adjacent protomers" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304" FT BINDING 63 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_note="ligand shared between two adjacent protomers" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304" FT BINDING 127 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_note="ligand shared between two adjacent protomers" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304" FT BINDING 157..159 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_note="ligand shared between two adjacent protomers" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304" FT BINDING 159 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="ligand shared between two adjacent protomers" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304" FT BINDING 174 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="ligand shared between two adjacent protomers" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304" FT BINDING 228 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_note="ligand shared between two adjacent protomers" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304" FT BINDING 238 FT /ligand="glycine" FT /ligand_id="ChEBI:CHEBI:57305" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304" SQ SEQUENCE 263 AA; 27873 MW; ADA793304C972638 CRC64; MSLDERIITQ AILETYFEKF KSSLDLDVAI VGGGPSGMTA ARLLAADGFN VALFERKLSL GGGMWGGGMT FNMIVVQEES VHLLTDVGVP VKRYKDNYFT ADAVAATTTL ASAACLAGAK IFNCMSVEDV MLREENGVKR VTGIVINSSP VEIAGLHVDP VVLGSKYLVE ATGHAVEVLQ TLVRKNDVRL NTPSGGIEGE QSMWADTAEI NTVKNTREIF PGLYVAGMAA NASYGSYRMG PIFGGMLLSG EKVAADIAAK LKG //