THIG_BACSU
ID THIG_BACSU Reviewed; 256 AA.
AC O31618;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Thiazole synthase;
DE EC=2.8.1.10 {ECO:0000269|PubMed:14567704};
GN Name=thiG; Synonyms=yjbT; OrderedLocusNames=BSU11690;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=168 / CU1065;
RX PubMed=14567704; DOI=10.1021/bi034902z;
RA Park J.-H., Dorrestein P.C., Zhai H., Kinsland C., McLafferty F.W.,
RA Begley T.P.;
RT "Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin
RT B1).";
RL Biochemistry 42:12430-12438(2003).
RN [3]
RP REACTION MECHANISM.
RX PubMed=15489164; DOI=10.1016/j.chembiol.2004.08.009;
RA Dorrestein P.C., Zhai H., McLafferty F.W., Begley T.P.;
RT "The biosynthesis of the thiazole phosphate moiety of thiamin: the sulfur
RT transfer mediated by the sulfur carrier protein ThiS.";
RL Chem. Biol. 11:1373-1381(2004).
RN [4]
RP REACTION MECHANISM, MUTAGENESIS OF LYS-98, AND ROLE OF LYS-98 IN SCHIFF
RP BASE FORMATION WITH DXP.
RC STRAIN=168 / CU1065;
RX PubMed=15012138; DOI=10.1021/ja039616p;
RA Dorrestein P.C., Zhai H., Taylor S.V., McLafferty F.W., Begley T.P.;
RT "The biosynthesis of the thiazole phosphate moiety of thiamin (vitamin B1):
RT the early steps catalyzed by thiazole synthase.";
RL J. Am. Chem. Soc. 126:3091-3096(2004).
RN [5]
RP REACTION PRODUCTS, AND REACTION MECHANISM.
RX PubMed=19216519; DOI=10.1021/ja806752h;
RA Hazra A., Chatterjee A., Begley T.P.;
RT "Biosynthesis of the thiamin thiazole in Bacillus subtilis: identification
RT of the product of the thiazole synthase-catalyzed reaction.";
RL J. Am. Chem. Soc. 131:3225-3229(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 3-255 IN COMPLEX WITH SULFUR
RP CARRIER PROTEIN THIS AND PHOSPHATE, MUTAGENESIS OF GLU-100 AND ASP-184,
RP SUBUNIT, AND REACTION MECHANISM.
RX PubMed=15362849; DOI=10.1021/bi0488911;
RA Settembre E.C., Dorrestein P.C., Zhai H., Chatterjee A., McLafferty F.W.,
RA Begley T.P., Ealick S.E.;
RT "Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole
RT synthase/sulfur carrier protein complex.";
RL Biochemistry 43:11647-11657(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-255.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of northeast structural genomics target sr156.";
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:0000269|PubMed:14567704}.
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;
CC Evidence={ECO:0000269|PubMed:14567704};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or ThiS.
CC {ECO:0000269|PubMed:15362849}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000305}.
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; AL009126; CAB13026.1; -; Genomic_DNA.
DR PIR; D69845; D69845.
DR RefSeq; NP_389051.1; NC_000964.3.
DR RefSeq; WP_010886483.1; NZ_JNCM01000035.1.
DR PDB; 1TYG; X-ray; 3.15 A; A/C=3-255.
DR PDB; 1XM3; X-ray; 1.80 A; A/B/C/D=1-255.
DR PDBsum; 1TYG; -.
DR PDBsum; 1XM3; -.
DR AlphaFoldDB; O31618; -.
DR SMR; O31618; -.
DR IntAct; O31618; 2.
DR MINT; O31618; -.
DR STRING; 224308.BSU11690; -.
DR PaxDb; O31618; -.
DR PRIDE; O31618; -.
DR EnsemblBacteria; CAB13026; CAB13026; BSU_11690.
DR GeneID; 936422; -.
DR KEGG; bsu:BSU11690; -.
DR eggNOG; COG2022; Bacteria.
DR InParanoid; O31618; -.
DR OMA; PHNFQLI; -.
DR PhylomeDB; O31618; -.
DR BioCyc; BSUB:BSU11690-MON; -.
DR BioCyc; MetaCyc:BSU11690-MON; -.
DR BRENDA; 2.8.1.10; 658.
DR UniPathway; UPA00060; -.
DR EvolutionaryTrace; O31618; -.
DR Proteomes; UP000001570; 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..256
FT /note="Thiazole synthase"
FT /id="PRO_0000162788"
FT ACT_SITE 98
FT /note="Schiff-base intermediate with DXP"
FT BINDING 159
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT BINDING 185..186
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT BINDING 207..208
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT MUTAGEN 98
FT /note="K->A: No activity; no imine formation with DXP."
FT /evidence="ECO:0000269|PubMed:15012138"
FT MUTAGEN 100
FT /note="E->A: Activity reduced 38-fold."
FT /evidence="ECO:0000269|PubMed:15362849"
FT MUTAGEN 184
FT /note="D->A: No activity."
FT /evidence="ECO:0000269|PubMed:15362849"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1XM3"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1XM3"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:1XM3"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:1XM3"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1XM3"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1TYG"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1TYG"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1XM3"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1XM3"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:1XM3"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1XM3"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1XM3"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:1XM3"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1XM3"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:1XM3"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1XM3"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1XM3"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:1XM3"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1XM3"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:1XM3"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:1XM3"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:1XM3"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1XM3"
FT HELIX 216..236
FT /evidence="ECO:0007829|PDB:1XM3"
SQ SEQUENCE 256 AA; 27022 MW; 39256F75262F97E6 CRC64;
MSMLTIGGKS FQSRLLLGTG KYPSFDIQKE AVAVSESDIL TFAVRRMNIF EASQPNFLEQ
LDLSKYTLLP NTAGASTAEE AVRIARLAKA SGLCDMIKVE VIGCSRSLLP DPVETLKASE
QLLEEGFIVL PYTSDDVVLA RKLEELGVHA IMPGASPIGS GQGILNPLNL SFIIEQAKVP
VIVDAGIGSP KDAAYAMELG ADGVLLNTAV SGADDPVKMA RAMKLAVEAG RLSYEAGRIP
LKQYGTASSP GEGLPV
