ID   TENA_STAHJ              Reviewed;         229 AA.
AC   Q4L7X6;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Aminopyrimidine aminohydrolase {ECO:0000250|UniProtKB:P25052};
DE            EC=3.5.99.2 {ECO:0000250|UniProtKB:Q6GEY1};
DE   AltName: Full=Thiaminase II {ECO:0000250|UniProtKB:Q6GEY1};
GN   Name=tenA; OrderedLocusNames=SH0940;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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). Is also able to catalyze the hydrolytic
CC       cleavage of thiamine; however, this thiaminase activity may not be
CC       physiologically relevant. Therefore, is probably involved in the
CC       regeneration of the thiamine pyrimidine from thiamine degraded products
CC       present in the environment, rather than in thiamine degradation.
CC       {ECO:0000250|UniProtKB:P25052, ECO:0000250|UniProtKB:Q6GEY1}.
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:0000250|UniProtKB:P25052};
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:0000250|UniProtKB:Q6GEY1};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000250|UniProtKB:P25052}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q6GEY1}.
CC   -!- SIMILARITY: Belongs to the TenA 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; AP006716; BAE04249.1; -; Genomic_DNA.
DR   RefSeq; WP_011275251.1; NC_007168.1.
DR   AlphaFoldDB; Q4L7X6; -.
DR   SMR; Q4L7X6; -.
DR   STRING; 279808.SH0940; -.
DR   EnsemblBacteria; BAE04249; BAE04249; SH0940.
DR   GeneID; 58062876; -.
DR   KEGG; sha:SH0940; -.
DR   eggNOG; COG0819; Bacteria.
DR   HOGENOM; CLU_077537_3_1_9; -.
DR   OMA; SAHHYIR; -.
DR   OrthoDB; 1537025at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000000543; Chromosome.
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   3: Inferred from homology;
KW   Hydrolase; Thiamine biosynthesis.
FT   CHAIN           1..229
FT                   /note="Aminopyrimidine aminohydrolase"
FT                   /id="PRO_0000293617"
FT   ACT_SITE        137
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P25052"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P25052"
FT   BINDING         44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P25052"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P25052"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P25052"
FT   SITE            47
FT                   /note="Increases nucleophilicity of active site Cys"
FT                   /evidence="ECO:0000250|UniProtKB:P25052"
SQ   SEQUENCE   229 AA;  26676 MW;  DB9ACFCAD9D633F1 CRC64;
     MTFSTEIKEA AQPIIEEIYN DGFIQDLLKG DLDAQAVRQY LRADASYLKE FTNLYALLIP
     KAPSMKDVKF LVEQIEFMLD GEVEAHEILA DYINEPYEEI VKEKVWPPSG DHYIKHMYYH
     AYAHENAAYT IAAMAPCPYV YEVVAKMALD DQNLNRDSVT SKWFDFYSTE MRPLIEVFDN
     LLDELTANCT EQEKKDIKES FLQSTIHERN FFNMAYINEQ WNFGGDKNA