ID   TENA_STACT              Reviewed;         228 AA.
AC   O54496; B9DMF8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 92.
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=Sca_1596;
OS   Staphylococcus carnosus (strain TM300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=396513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Krismer B., Goetz F.;
RT   "Identification of an operon involved in thiamin biosynthesis in
RT   Staphylococcus carnosus TM300.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM300;
RX   PubMed=19060169; DOI=10.1128/aem.01982-08;
RA   Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA   Goetz F.;
RT   "Genome analysis of the meat starter culture bacterium Staphylococcus
RT   carnosus TM300.";
RL   Appl. Environ. Microbiol. 75:811-822(2009).
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}.
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DR   EMBL; AF109218; AAF25541.1; -; Genomic_DNA.
DR   EMBL; AM295250; CAL28501.1; -; Genomic_DNA.
DR   RefSeq; WP_015900841.1; NC_012121.1.
DR   AlphaFoldDB; O54496; -.
DR   SMR; O54496; -.
DR   STRING; 396513.SCA_1596; -.
DR   GeneID; 60544692; -.
DR   KEGG; sca:SCA_1596; -.
DR   eggNOG; COG0819; Bacteria.
DR   HOGENOM; CLU_077537_3_1_9; -.
DR   OMA; SAHHYIR; -.
DR   OrthoDB; 1537025at2; -.
DR   BioCyc; SCAR396513:SCA_RS08105-MON; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000000444; 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..228
FT                   /note="Aminopyrimidine aminohydrolase"
FT                   /id="PRO_0000293614"
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   228 AA;  26785 MW;  02EA2FB6B810E58D CRC64;
     MNFAETLERD AQPIIDEIYQ DHFIQELLKG DIKKEALRQY LRADASYLRE FANIYALLIP
     IMPDLESVRF LVDQIQFIVN GEVEAHEYMA DYIGENYNEI VQKKVWPPSG DHYIKHMYYN
     VYAHENAAYA IAAMAPCPYV YAMIAKRAMK DPNLNKSSIL AKWFEFYNTE MDPLIEVLDD
     LMNQLTANMS ETEKNEVREN YLQSTVHELN FFNMAYTSEK WQFGGERV