ID THI4_DESMR Reviewed; 263 AA. AC C4XIR5; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 05-JUN-2019, entry version 63. 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}; GN OrderedLocusNames=DMR_31420; OS Desulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. 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., RA Aoki N., Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., RA Takeyama H., Matsunaga T.; RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 RT revealed 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 CC (ADT), an adenylated thiazole intermediate, using free sulfide as CC a source of 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 SMR; C4XIR5; -. DR STRING; 573370.DMR_31420; -. DR PRIDE; C4XIR5; -. DR EnsemblBacteria; BAH76633; BAH76633; DMR_31420. DR KEGG; dma:DMR_31420; -. DR eggNOG; ENOG4105IQJ; Bacteria. DR eggNOG; COG1635; LUCA. DR HOGENOM; HOG000106048; -. DR KO; K22699; -. DR OMA; MWGGGMM; -. DR BioCyc; DMAG573370:GHJL-3184-MONOMER; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000009071; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. 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; -; 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 SUPFAM; SSF51905; SSF51905; 1. DR TIGRFAMs; TIGR00292; TIGR00292; 1. PE 3: Inferred from homology; KW Complete proteome; Iron; Metal-binding; NAD; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 263 Thiamine thiazole synthase. FT /FTId=PRO_1000205004. FT NP_BIND 55 56 NAD. {ECO:0000255|HAMAP-Rule:MF_00304}. FT NP_BIND 157 159 NAD; shared with adjacent protomer. FT {ECO:0000255|HAMAP-Rule:MF_00304}. FT METAL 159 159 Iron; shared with adjacent protomer. FT {ECO:0000255|HAMAP-Rule:MF_00304}. FT METAL 174 174 Iron. {ECO:0000255|HAMAP-Rule:MF_00304}. FT BINDING 36 36 NAD. {ECO:0000255|HAMAP-Rule:MF_00304}. FT BINDING 63 63 NAD; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00304}. FT BINDING 127 127 NAD; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00304}. FT BINDING 228 228 NAD; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00304}. FT BINDING 238 238 Glycine. {ECO:0000255|HAMAP- FT 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 //