THIG_THET8
ID THIG_THET8 Reviewed; 268 AA.
AC Q5SKG7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=TTHA0676;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of ttha0676 from Thermus thermophilus HB8.";
RL Submitted (FEB-2009) to the PDB data bank.
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=1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-
CC carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-
CC carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-
CC carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O;
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}.
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DR EMBL; AP008226; BAD70499.1; -; Genomic_DNA.
DR RefSeq; WP_011228115.1; NC_006461.1.
DR RefSeq; YP_143942.1; NC_006461.1.
DR PDB; 2HTM; X-ray; 2.30 A; A/B/C/D=1-268.
DR PDBsum; 2HTM; -.
DR AlphaFoldDB; Q5SKG7; -.
DR SMR; Q5SKG7; -.
DR STRING; 300852.55772058; -.
DR EnsemblBacteria; BAD70499; BAD70499; BAD70499.
DR GeneID; 3168363; -.
DR KEGG; ttj:TTHA0676; -.
DR PATRIC; fig|300852.9.peg.670; -.
DR eggNOG; COG2022; Bacteria.
DR HOGENOM; CLU_062233_1_0_0; -.
DR OMA; PHNFQLI; -.
DR PhylomeDB; Q5SKG7; -.
DR UniPathway; UPA00060; -.
DR EvolutionaryTrace; Q5SKG7; -.
DR Proteomes; UP000000532; Chromosome.
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-UniPathway.
DR CDD; cd04728; ThiG; 1.
DR Gene3D; 3.20.20.70; -; 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; PTHR34266; 1.
DR Pfam; PF05690; ThiG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Schiff base;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..268
FT /note="Thiazole synthase"
FT /id="PRO_0000162869"
FT REGION 238..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 185..186
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 207..208
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:2HTM"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2HTM"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:2HTM"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:2HTM"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:2HTM"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:2HTM"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:2HTM"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:2HTM"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:2HTM"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2HTM"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2HTM"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:2HTM"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:2HTM"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:2HTM"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2HTM"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:2HTM"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:2HTM"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:2HTM"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:2HTM"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:2HTM"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:2HTM"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:2HTM"
FT HELIX 216..236
FT /evidence="ECO:0007829|PDB:2HTM"
SQ SEQUENCE 268 AA; 28449 MW; D099F3FB26F4AAB6 CRC64;
MDTWKVGPVE LKSRLILGSG KYEDFGVMRE AIAAAKAEVV TVSVRRVELK APGHVGLLEA
LEGVRLLPNT AGARTAEEAV RLARLGRLLT GERWVKLEVI PDPTYLLPDP LETLKAAERL
IEEDFLVLPY MGPDLVLAKR LAALGTATVM PLAAPIGSGW GVRTRALLEL FAREKASLPP
VVVDAGLGLP SHAAEVMELG LDAVLVNTAI AEAQDPPAMA EAFRLAVEAG RKAYLAGPMR
PREAASPSSP VEGVPFTPTG PRPGRGPQ
