THIG_DEIRA
ID THIG_DEIRA Reviewed; 267 AA.
AC Q9RYY1;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 123.
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=DR_A0172;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF12198.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE001825; AAF12198.1; ALT_INIT; Genomic_DNA.
DR PIR; G75613; G75613.
DR RefSeq; NP_285496.1; NC_001264.1.
DR RefSeq; WP_027479758.1; NC_001264.1.
DR AlphaFoldDB; Q9RYY1; -.
DR SMR; Q9RYY1; -.
DR STRING; 243230.DR_A0172; -.
DR EnsemblBacteria; AAF12198; AAF12198; DR_A0172.
DR KEGG; dra:DR_A0172; -.
DR PATRIC; fig|243230.17.peg.3060; -.
DR eggNOG; COG2022; Bacteria.
DR HOGENOM; CLU_062233_1_0_0; -.
DR InParanoid; Q9RYY1; -.
DR OMA; PHNFQLI; -.
DR OrthoDB; 784095at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000002524; Chromosome II.
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 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Schiff base; Thiamine biosynthesis;
KW Transferase.
FT CHAIN 1..267
FT /note="Thiazole synthase"
FT /id="PRO_0000162813"
FT REGION 243..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 162
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 188..189
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 210..211
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
SQ SEQUENCE 267 AA; 27590 MW; A4ED02A2D37DAA98 CRC64;
MNTNDLLTIG GQSFSSRLLL GTGKYRDFAV MQDALGASGT QIVTVAIRRV ELKAPGHDGL
LDALDLDRFQ LLPNTAGCRT AEEAVRVAKL ARAATGVSWL KLEVIPDPKY LLPDPIGTLR
AAEILVGEGF TVLPYVQPDG VLARALEAVG CATVMPLASP IGTGKGLRTP ELIRTVIDGA
GVPIVVDAGL GVPSDAAQAL ELGADAVLVN TAIAEARDPV AMARAFALGV EAGRLGYLAG
RMQQRDSASP SSPAAGVVRL PDPEVPA
