ID THIG_AGRFC Reviewed; 257 AA. AC Q8UCD2; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-NOV-2024, entry version 103. DE RecName: Full=Thiazole synthase {ECO:0000255|HAMAP-Rule:MF_00443}; DE EC=2.8.1.10 {ECO:0000255|HAMAP-Rule:MF_00443}; GN Name=thiG {ECO:0000255|HAMAP-Rule:MF_00443}; OrderedLocusNames=Atu2566; GN ORFNames=AGR_C_4650; OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens OS (strain C58)). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=176299; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970; RX PubMed=11743193; DOI=10.1126/science.1066804; RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., RA Gordon M.P., Olson M.V., Nester E.W.; RT "The genome of the natural genetic engineer Agrobacterium tumefaciens RT C58."; RL Science 294:2317-2323(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970; RX PubMed=11743194; DOI=10.1126/science.1066803; RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M., RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.; RT "Genome sequence of the plant pathogen and biotechnology agent RT Agrobacterium tumefaciens C58."; RL Science 294:2323-2328(2001). CC -!- FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate CC (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is CC provided by the thiocarboxylate moiety of the carrier protein ThiS. In CC vitro, sulfur can be provided by H(2)S. {ECO:0000255|HAMAP- CC Rule:MF_00443}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH + CC 2-iminoacetate + 1-deoxy-D-xylulose 5-phosphate = [sulfur-carrier CC protein ThiS]-C-terminal Gly-Gly + 2-[(2R,5Z)-2-carboxy-4- CC methylthiazol-5(2H)-ylidene]ethyl phosphate + 2 H2O + 2 H(+); CC Xref=Rhea:RHEA:26297, Rhea:RHEA-COMP:12908, Rhea:RHEA-COMP:12909, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57792, CC ChEBI:CHEBI:62899, ChEBI:CHEBI:77846, ChEBI:CHEBI:90619, CC ChEBI:CHEBI:90778; EC=2.8.1.10; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00443}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00443}. CC -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or ThiS. CC {ECO:0000255|HAMAP-Rule:MF_00443}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00443}. CC -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000255|HAMAP- CC Rule:MF_00443}. 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; AE007869; AAK88290.1; -; Genomic_DNA. DR PIR; A97667; A97667. DR PIR; AE2891; AE2891. DR RefSeq; NP_355505.1; NC_003062.2. DR RefSeq; WP_010972406.1; NC_003062.2. DR AlphaFoldDB; Q8UCD2; -. DR SMR; Q8UCD2; -. DR STRING; 176299.Atu2566; -. DR EnsemblBacteria; AAK88290; AAK88290; Atu2566. DR KEGG; atu:Atu2566; -. DR PATRIC; fig|176299.10.peg.2570; -. DR eggNOG; COG2022; Bacteria. DR HOGENOM; CLU_062233_1_0_5; -. DR OrthoDB; 9805935at2; -. DR PhylomeDB; Q8UCD2; -. DR BioCyc; AGRO:ATU2566-MONOMER; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000000813; Chromosome circular. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:1990107; F:thiazole synthase activity; IEA:RHEA. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd04728; ThiG; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_00443; ThiG; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR033983; Thiazole_synthase_ThiG. DR InterPro; IPR008867; ThiG. DR PANTHER; PTHR34266; THIAZOLE SYNTHASE; 1. DR PANTHER; PTHR34266:SF2; THIAZOLE SYNTHASE; 1. DR Pfam; PF05690; ThiG; 1. DR SUPFAM; SSF110399; ThiG-like; 1. PE 3: Inferred from homology; KW Cytoplasm; Reference proteome; Schiff base; Thiamine biosynthesis; KW Transferase. FT CHAIN 1..257 FT /note="Thiazole synthase" FT /id="PRO_0000162775" FT ACT_SITE 96 FT /note="Schiff-base intermediate with DXP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443" FT BINDING 157 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443" FT BINDING 184..185 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443" FT BINDING 206..207 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443" SQ SEQUENCE 257 AA; 27582 MW; 672B2E43C6D40F34 CRC64; MLTLYGREVS SRLLLGTARY PSPAVLADAV RASNTDILTI SLRREMAGAK KGGQFFELIR ELDRHILPNT AGCHTAKEAV LTAKMAREVF RTDWIKLEVI GHHDTLQPDV FALVEAAKIL CDEGFEVFPY TTDDLVVAEK LLEAGCRVLM PWCAPIGSAM GPLNLTALKS MRARFPEVPL IVDAGIGRPS HAVTVMELGY DAVLLNTAVA GAGDPVGMAE AFARAIEAGH QAYLSGPLEP RDMAVPSTPV IGTAVFS //