TENA_STAAB
ID TENA_STAAB Reviewed; 229 AA.
AC Q2YUL0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=SAB1978c;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI81667.1; -; Genomic_DNA.
DR RefSeq; WP_000396070.1; NC_007622.1.
DR AlphaFoldDB; Q2YUL0; -.
DR SMR; Q2YUL0; -.
DR KEGG; sab:SAB1978c; -.
DR HOGENOM; CLU_077537_3_1_9; -.
DR OMA; SAHHYIR; -.
DR UniPathway; UPA00060; -.
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_0000293605"
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; 26859 MW; 38B2DFFF467FC8C5 CRC64;
MEFSQKLYQA AKPIINDIYE DDFIQKMLLG NIQADALRHY LQADAAYLKE FTNLYALLIP
KMNSMNDVKF LVEQIEFMVE GEVLAHDILA QIVGESYEEI INTKFWPPSG DHYIKHMYFQ
AHSRENAIYT IAAMAPCPYI YAELAKRSQS DHKLNREKDT AKWFDFYSTE MDDIINVFEA
LMNKLAESMS DKELEQVKQV FLESCIHERR FFNMAMTLEQ WEFGGKVND