TENA_BACSU
ID TENA_BACSU Reviewed; 236 AA.
AC P25052;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Aminopyrimidine aminohydrolase {ECO:0000303|PubMed:17618314};
DE EC=3.5.99.2 {ECO:0000269|PubMed:17618314};
DE AltName: Full=4-amino-5-aminomethyl-2-methylpyrimidine hydrolase {ECO:0000303|PubMed:17618314};
DE AltName: Full=Thiaminase II {ECO:0000303|PubMed:15709744};
GN Name=tenA {ECO:0000303|PubMed:1898926}; OrderedLocusNames=BSU11650;
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17618314; DOI=10.1038/nchembio.2007.13;
RA Jenkins A.H., Schyns G., Potot S., Sun G., Begley T.P.;
RT "A new thiamin salvage pathway.";
RL Nat. Chem. Biol. 3:492-497(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH HMP PRODUCT.
RA Rajan S.S., Shuvalova L., Yang X., Hussar C., Collart F., Anderson W.F.;
RT "Crystal structure of THI-4 protein from Bacillus subtilis.";
RL Submitted (JUN-2004) to the PDB data bank.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 2-236.
RA Eswaramoorthy S., Swaminathan S.;
RT "Crystal structure of transcriptional activator tenA from Bacillus
RT subtilis.";
RL Submitted (JUL-2004) to the PDB data bank.
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH HMP
RP PRODUCT.
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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT PHE-112 IN COMPLEX WITH
RP SUBSTRATE ANALOG, REACTION MECHANISM, ACTIVE SITE, AND MUTAGENESIS OF
RP ASP-44; TYR-47; TYR-112; CYS-135 AND GLU-205.
RX PubMed=18054064; DOI=10.1016/j.bioorg.2007.10.005;
RA Jenkins A.L., Zhang Y., Ealick S.E., Begley T.P.;
RT "Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus
RT subtilis.";
RL Bioorg. Chem. 36:29-32(2008).
CC -!- FUNCTION: Catalyzes an amino-pyrimidine hydrolysis reaction at the C5'
CC of the pyrimidine moiety of thiamine compounds, a reaction that is part
CC of a thiamine salvage pathway. Thus, catalyzes the conversion of 4-
CC amino-5-aminomethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2-
CC methylpyrimidine (HMP). To a lesser extent, is also able to catalyze
CC the hydrolytic cleavage of thiamine; however, this thiaminase activity
CC is unlikely to be physiologically relevant. Therefore, is involved in
CC the regeneration of the thiamine pyrimidine from thiamine degraded
CC products present in the environment, rather than in thiamine
CC degradation. {ECO:0000269|PubMed:17618314}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-
CC hydroxymethyl-2-methylpyrimidine + NH4(+); Xref=Rhea:RHEA:31799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16892, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:63416; EC=3.5.99.2;
CC Evidence={ECO:0000269|PubMed:17618314};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + thiamine = 4-amino-5-hydroxymethyl-2-methylpyrimidine +
CC 5-(2-hydroxyethyl)-4-methylthiazole + H(+); Xref=Rhea:RHEA:17509,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC ChEBI:CHEBI:17957, ChEBI:CHEBI:18385; EC=3.5.99.2;
CC Evidence={ECO:0000269|PubMed:17618314};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.8 uM for 4-amino-5-aminomethyl-2-methylpyrimidine
CC {ECO:0000269|PubMed:17618314};
CC Note=kcat is 22.0 min(-1) for the hydrolysis of 4-amino-5-
CC aminomethyl-2-methylpyrimidine. Catalyzes the hydrolysis of
CC aminopyrimidine 100 times faster than the hydrolysis of thiamine.
CC {ECO:0000269|PubMed:17618314};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000269|PubMed:17618314}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000303|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 (PubMed:1898926). The deletion mutant does not
CC require a hydroxypyrimidine source as it is able to biosynthesize it
CC using ThiA; the tenA/thiA double mutant, however, is hydroxypyrimidine-
CC requiring and is unable to salvage the pyrimidine from
CC formylaminopyrimidine, aminopyrimidine, or base-degraded thiamine
CC (PubMed:17618314). {ECO:0000269|PubMed:17618314,
CC ECO:0000269|PubMed:1898926}.
CC -!- SIMILARITY: Belongs to the TenA 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; AAA22848.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13022.1; -; Genomic_DNA.
DR PIR; A39184; XMBSTA.
DR RefSeq; NP_389047.1; NC_000964.3.
DR RefSeq; WP_003232909.1; NZ_JNCM01000035.1.
DR PDB; 1TO9; X-ray; 2.40 A; A/B=1-236.
DR PDB; 1TYH; X-ray; 2.54 A; A/B/D/E=2-236.
DR PDB; 1YAF; X-ray; 2.60 A; A/B/C/D=1-236.
DR PDB; 1YAK; X-ray; 2.50 A; A/B/C/D=1-236.
DR PDB; 2QCX; X-ray; 2.20 A; A/B=1-236.
DR PDBsum; 1TO9; -.
DR PDBsum; 1TYH; -.
DR PDBsum; 1YAF; -.
DR PDBsum; 1YAK; -.
DR PDBsum; 2QCX; -.
DR AlphaFoldDB; P25052; -.
DR SMR; P25052; -.
DR IntAct; P25052; 1.
DR MINT; P25052; -.
DR STRING; 224308.BSU11650; -.
DR DrugBank; DB02022; 4-Amino-5-Hydroxymethyl-2-Methylpyrimidine.
DR PaxDb; P25052; -.
DR PRIDE; P25052; -.
DR DNASU; 939807; -.
DR EnsemblBacteria; CAB13022; CAB13022; BSU_11650.
DR GeneID; 939807; -.
DR KEGG; bsu:BSU11650; -.
DR PATRIC; fig|224308.179.peg.1254; -.
DR eggNOG; COG0819; Bacteria.
DR InParanoid; P25052; -.
DR OMA; FYIIQDY; -.
DR PhylomeDB; P25052; -.
DR BioCyc; BSUB:BSU11650-MON; -.
DR BioCyc; MetaCyc:BSU11650-MON; -.
DR BRENDA; 3.5.99.2; 658.
DR UniPathway; UPA00060; -.
DR EvolutionaryTrace; P25052; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050334; F:thiaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.910.10; -; 1.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
DR InterPro; IPR027574; Thiaminase_II.
DR Pfam; PF03070; TENA_THI-4; 1.
DR SUPFAM; SSF48613; SSF48613; 1.
DR TIGRFAMs; TIGR04306; salvage_TenA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome; Thiamine biosynthesis.
FT CHAIN 1..236
FT /note="Aminopyrimidine aminohydrolase"
FT /id="PRO_0000192046"
FT ACT_SITE 135
FT /note="Nucleophile"
FT /evidence="ECO:0000303|PubMed:18054064"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000303|PubMed:18054064"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15709744, ECO:0000269|Ref.5"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15709744, ECO:0000269|Ref.5"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15709744, ECO:0000269|Ref.5"
FT SITE 47
FT /note="Increases nucleophilicity of active site Cys"
FT /evidence="ECO:0000303|PubMed:18054064"
FT MUTAGEN 44
FT /note="D->A: 6300-fold reduction in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:18054064"
FT MUTAGEN 47
FT /note="Y->F: About 2-fold decrease in substrate affinity
FT and 30-fold reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18054064"
FT MUTAGEN 112
FT /note="Y->F: About 2-fold decrease in substrate affinity
FT and 70-fold reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18054064"
FT MUTAGEN 135
FT /note="C->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:18054064"
FT MUTAGEN 205
FT /note="E->A: 2000-fold reduction in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:18054064"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:2QCX"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:2QCX"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:2QCX"
FT HELIX 34..61
FT /evidence="ECO:0007829|PDB:2QCX"
FT HELIX 65..93
FT /evidence="ECO:0007829|PDB:2QCX"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:2QCX"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:2QCX"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2QCX"
FT HELIX 125..146
FT /evidence="ECO:0007829|PDB:2QCX"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:2QCX"
FT HELIX 166..184
FT /evidence="ECO:0007829|PDB:2QCX"
FT HELIX 188..213
FT /evidence="ECO:0007829|PDB:2QCX"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:2QCX"
SQ SEQUENCE 236 AA; 27417 MW; 6815CFC95BDB07D6 CRC64;
MKFSEECRSA AAEWWEGSFV HPFVQGIGDG TLPIDRFKYY VLQDSYYLTH FAKVQSFGAA
YAKDLYTTGR MASHAQGTYE AEMALHREFA ELLEISEEER KAFKPSPTAY SYTSHMYRSV
LSGNFAEILA ALLPCYWLYY EVGEKLLHCD PGHPIYQKWI GTYGGDWFRQ QVEEQINRFD
ELAENSTEEV RAKMKENFVI SSYYEYQFWG MAYRKEGWSD SAIKEVEECG ASRHNG
