ID   TENA_STAEQ              Reviewed;         229 AA.
AC   Q5HMC7;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=SERP1701;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000029; AAW55079.1; -; Genomic_DNA.
DR   RefSeq; WP_001829894.1; NC_002976.3.
DR   AlphaFoldDB; Q5HMC7; -.
DR   SMR; Q5HMC7; -.
DR   STRING; 176279.SERP1701; -.
DR   EnsemblBacteria; AAW55079; AAW55079; SERP1701.
DR   GeneID; 50018207; -.
DR   KEGG; ser:SERP1701; -.
DR   eggNOG; COG0819; Bacteria.
DR   HOGENOM; CLU_077537_3_1_9; -.
DR   OMA; SAHHYIR; -.
DR   OrthoDB; 1537025at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Thiamine biosynthesis.
FT   CHAIN           1..229
FT                   /note="Aminopyrimidine aminohydrolase"
FT                   /id="PRO_0000293616"
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;  26900 MW;  C520C51829A236B2 CRC64;
     MTFSKELREA SRPIIDDIYN DGFIQDLLAG KLSNQAVRQY LRADASYLKE FTNIYAMLIP
     KMSSMEDVKF LVEQIEFMLE GEVEAHEVLA DFINEPYEEI VKEKVWPPSG DHYIKHMYFN
     AFARENAAFT IAAMAPCPYV YAVIGKRAME DPKLNKESVT SKWFQFYSTE MDELVDVFDQ
     LMDRLTKHCS ETEKKEIKEN FLQSTIHERH FFNMAYINEK WEYGGNNNE