TENA_STAES
ID TENA_STAES Reviewed; 229 AA.
AC Q8CNK1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=SE_1693;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a putative thiaminase II (SE1693) from Staphylococcus
RT epidermidis ATCC 12228 at 1.65 A resolution.";
RL Submitted (JUN-2010) to the PDB data bank.
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:0000269|Ref.2}.
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; AE015929; AAO05292.1; -; Genomic_DNA.
DR RefSeq; NP_765248.1; NC_004461.1.
DR RefSeq; WP_001829894.1; NZ_WBME01000021.1.
DR PDB; 3NO6; X-ray; 1.65 A; A/B/C/D=1-229.
DR PDBsum; 3NO6; -.
DR AlphaFoldDB; Q8CNK1; -.
DR SMR; Q8CNK1; -.
DR STRING; 176280.SE_1693; -.
DR DNASU; 1057810; -.
DR EnsemblBacteria; AAO05292; AAO05292; SE_1693.
DR GeneID; 50018207; -.
DR KEGG; sep:SE_1693; -.
DR PATRIC; fig|176280.10.peg.1653; -.
DR eggNOG; COG0819; Bacteria.
DR HOGENOM; CLU_077537_3_1_9; -.
DR OMA; SAHHYIR; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000001411; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Thiamine biosynthesis.
FT CHAIN 1..229
FT /note="Aminopyrimidine aminohydrolase"
FT /id="PRO_0000293615"
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"
FT HELIX 3..20
FT /evidence="ECO:0007829|PDB:3NO6"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:3NO6"
FT HELIX 34..58
FT /evidence="ECO:0007829|PDB:3NO6"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3NO6"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:3NO6"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:3NO6"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:3NO6"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:3NO6"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:3NO6"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:3NO6"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:3NO6"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:3NO6"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:3NO6"
FT HELIX 191..217
FT /evidence="ECO:0007829|PDB:3NO6"
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
