TENI_BACSU
ID TENI_BACSU Reviewed; 205 AA.
AC P25053;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Thiazole tautomerase {ECO:0000303|PubMed:21534620};
DE EC=5.3.99.10 {ECO:0000269|PubMed:21534620};
GN Name=tenI {ECO:0000303|PubMed:1898926}; OrderedLocusNames=BSU11660;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX PubMed=1898926; DOI=10.1128/jb.173.1.46-54.1991;
RA Pang A.S.-H., Nathoo S., Wong S.-L.;
RT "Cloning and characterization of a pair of novel genes that regulate
RT production of extracellular enzymes in Bacillus subtilis.";
RL J. Bacteriol. 173:46-54(1991).
RN [2]
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 [3]
RP INDUCTION.
RX PubMed=11717296; DOI=10.1128/jb.183.24.7371-7380.2001;
RA Lee J.M., Zhang S., Saha S., Santa Anna S., Jiang C., Perkins J.;
RT "RNA expression analysis using an antisense Bacillus subtilis genome
RT array.";
RL J. Bacteriol. 183:7371-7380(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RX PubMed=15709744; DOI=10.1021/bi0478648;
RA Toms A.V., Haas A.L., Park J.-H., Begley T.P., Ealick S.E.;
RT "Structural characterization of the regulatory proteins TenA and TenI from
RT Bacillus subtilis and identification of TenA as a thiaminase II.";
RL Biochemistry 44:2319-2329(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEX WITH REACTION PRODUCT,
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, ACTIVE SITE, AND
RP MUTAGENESIS OF HIS-122.
RX PubMed=21534620; DOI=10.1021/ja1110514;
RA Hazra A.B., Han Y., Chatterjee A., Zhang Y., Lai R.Y., Ealick S.E.,
RA Begley T.P.;
RT "A missing enzyme in thiamin thiazole biosynthesis: identification of TenI
RT as a thiazole tautomerase.";
RL J. Am. Chem. Soc. 133:9311-9319(2011).
CC -!- FUNCTION: Catalyzes the irreversible aromatization of 2-((2R,5Z)-2-
CC carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate (cThz*-P) to 2-
CC (2-carboxy-4-methylthiazol-5-yl)ethyl phosphate (cThz-P), a step in the
CC biosynthesis of the thiazole phosphate moiety of thiamine. Cannot use
CC cThz* as substrate, indicating that the phosphate group is essential.
CC Has no thiamine phosphate synthase activity, despite a high sequence
CC similarity with ThiE. {ECO:0000269|PubMed:21534620}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl
CC phosphate = 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate;
CC Xref=Rhea:RHEA:31459, ChEBI:CHEBI:62890, ChEBI:CHEBI:62899;
CC EC=5.3.99.10; Evidence={ECO:0000269|PubMed:21534620};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000303|PubMed:21534620}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15709744}.
CC -!- INDUCTION: Strongly repressed by thiamine.
CC {ECO:0000269|PubMed:11717296}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of this gene causes a delay in
CC sporulation, but does not affect cell growth and the production of
CC extracellular enzymes. {ECO:0000269|PubMed:1898926}.
CC -!- SIMILARITY: Belongs to the thiazole tautomerase family. {ECO:0000305}.
CC -!- CAUTION: Was originally described as a regulatory protein involved in
CC the regulation of the production of extracellular enzymes.
CC {ECO:0000303|PubMed:1898926, ECO:0000305}.
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DR EMBL; M73546; AAA22849.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13023.1; -; Genomic_DNA.
DR PIR; B39184; XMBSTI.
DR RefSeq; NP_389048.1; NC_000964.3.
DR RefSeq; WP_003232908.1; NZ_JNCM01000035.1.
DR PDB; 1YAD; X-ray; 2.10 A; A/B/C/D=1-205.
DR PDB; 3QH2; X-ray; 2.23 A; A/B/C/D=1-205.
DR PDBsum; 1YAD; -.
DR PDBsum; 3QH2; -.
DR AlphaFoldDB; P25053; -.
DR SMR; P25053; -.
DR STRING; 224308.BSU11660; -.
DR DrugBank; DB03570; Tris-Hydroxymethyl-Methyl-Ammonium.
DR jPOST; P25053; -.
DR PaxDb; P25053; -.
DR PRIDE; P25053; -.
DR EnsemblBacteria; CAB13023; CAB13023; BSU_11660.
DR GeneID; 936411; -.
DR KEGG; bsu:BSU11660; -.
DR PATRIC; fig|224308.179.peg.1255; -.
DR eggNOG; COG0352; Bacteria.
DR InParanoid; P25053; -.
DR OMA; EVDFIHI; -.
DR PhylomeDB; P25053; -.
DR BioCyc; BSUB:BSU11660-MON; -.
DR BioCyc; MetaCyc:BSU11660-MON; -.
DR UniPathway; UPA00060; -.
DR EvolutionaryTrace; P25053; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IBA:GO_Central.
DR GO; GO:0009228; P:thiamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR Pfam; PF02581; TMP-TENI; 1.
DR SUPFAM; SSF51391; SSF51391; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome; Thiamine biosynthesis.
FT CHAIN 1..205
FT /note="Thiazole tautomerase"
FT /id="PRO_0000157087"
FT ACT_SITE 122
FT /note="Proton acceptor"
FT /evidence="ECO:0000303|PubMed:21534620"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21534620"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21534620"
FT BINDING 176..177
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21534620"
FT MUTAGEN 122
FT /note="H->Q,A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:21534620"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1YAD"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:1YAD"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1YAD"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:1YAD"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:1YAD"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1YAD"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1YAD"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:1YAD"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1YAD"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1YAD"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:1YAD"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1YAD"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:1YAD"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:1YAD"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:1YAD"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1YAD"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1YAD"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:1YAD"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:1YAD"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:1YAD"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1YAD"
FT HELIX 185..199
FT /evidence="ECO:0007829|PDB:1YAD"
SQ SEQUENCE 205 AA; 22929 MW; B04749ED70F0A088 CRC64;
MELHAITDDS KPVEELARII ITIQNEVDFI HIRERSKSAA DILKLLDLIF EGGIDKRKLV
MNGRVDIALF STIHRVQLPS GSFSPKQIRA RFPHLHIGRS VHSLEEAVQA EKEDADYVLF
GHVFETDCKK GLEGRGVSLL SDIKQRISIP VIAIGGMTPD RLRDVKQAGA DGIAVMSGIF
SSAEPLEAAR RYSRKLKEMR YEKAL
