TENA_ALKHC
ID TENA_ALKHC Reviewed; 224 AA.
AC Q9K9G8;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Aminopyrimidine aminohydrolase {ECO:0000303|PubMed:17618314};
DE EC=3.5.99.2 {ECO:0000269|PubMed:17618314};
DE AltName: Full=4-amino-5-aminomethyl-2-methylpyrimidine hydrolase {ECO:0000303|PubMed:17618314};
GN Name=tenA {ECO:0000303|PubMed:17618314};
GN OrderedLocusNames=BH2679 {ECO:0000312|EMBL:BAB06398.1};
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=17618314; DOI=10.1038/nchembio.2007.13;
RA Jenkins A.H., Schyns G., Potot S., Sun G., Begley T.P.;
RT "A new thiamin salvage pathway.";
RL Nat. Chem. Biol. 3:492-497(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). To a lesser extent, is also able to catalyze
CC the hydrolytic cleavage of thiamine; however, this thiaminase activity
CC is unlikely to be physiologically relevant. Therefore, is involved in
CC the regeneration of the thiamine pyrimidine from thiamine degraded
CC products present in the environment, rather than in thiamine
CC degradation. {ECO:0000250|UniProtKB:P25052,
CC ECO:0000269|PubMed:17618314}.
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:0000269|PubMed:17618314};
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:P25052};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000269|PubMed:17618314}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P25052}.
CC -!- SIMILARITY: Belongs to the TenA family. {ECO:0000305}.
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DR EMBL; BA000004; BAB06398.1; -; Genomic_DNA.
DR PIR; G83984; G83984.
DR RefSeq; WP_010898828.1; NC_002570.2.
DR AlphaFoldDB; Q9K9G8; -.
DR SMR; Q9K9G8; -.
DR STRING; 272558.10175300; -.
DR EnsemblBacteria; BAB06398; BAB06398; BAB06398.
DR KEGG; bha:BH2679; -.
DR eggNOG; COG0819; Bacteria.
DR HOGENOM; CLU_077537_3_0_9; -.
DR OMA; PCMWGYS; -.
DR OrthoDB; 1537025at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000001258; 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; IPR026285; TenA_E.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
DR InterPro; IPR027574; Thiaminase_II.
DR Pfam; PF03070; TENA_THI-4; 1.
DR PIRSF; PIRSF003170; Pet18p; 1.
DR SUPFAM; SSF48613; SSF48613; 1.
DR TIGRFAMs; TIGR04306; salvage_TenA; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome; Thiamine biosynthesis.
FT CHAIN 1..224
FT /note="Aminopyrimidine aminohydrolase"
FT /id="PRO_0000431513"
FT ACT_SITE 135
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT BINDING 165
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 224 AA; 25585 MW; 86FFC77207A72852 CRC64;
MSFAASLYEK AQPIWEAGYN HPFVQGIGDG SLEKSKFQFF MKQDYLYLID YARLFALGTL
KGNDLQTMST FSKLLHATLN VEMDLHRAYA KRLGISAEEL EAIEPAATTL AYTSYMLNVA
QRGSLLDLIA AVLPCTWSYY EIGVKLKGIP GASDHPFYGE WIKLYASDEF KELADWLIQM
LDEEAKGLSS KEKAKLETIF LTTSRLENEF WDMAYNERMW NYNG
