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Database: UniProt/TrEMBL
Entry: Q5WK97_BACSK
LinkDB: Q5WK97_BACSK
Original site: Q5WK97_BACSK 
ID   Q5WK97_BACSK            Unreviewed;       223 AA.
AC   Q5WK97;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   20-JAN-2016, entry version 62.
DE   RecName: Full=Aminopyrimidine aminohydrolase {ECO:0000256|PIRNR:PIRNR003170};
DE            EC=3.5.99.2 {ECO:0000256|PIRNR:PIRNR003170};
GN   Name=tenA {ECO:0000313|EMBL:BAD63208.1};
GN   OrderedLocusNames=ABC0669 {ECO:0000313|EMBL:BAD63208.1};
OS   Bacillus clausii (strain KSM-K16).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=66692 {ECO:0000313|EMBL:BAD63208.1, ECO:0000313|Proteomes:UP000001168};
RN   [1] {ECO:0000313|Proteomes:UP000001168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16 {ECO:0000313|Proteomes:UP000001168};
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii
RT   KSM-K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes an amino-pyrimidine hydrolysis reaction at the
CC       C5' of the pyrimidine moiety of thiamine compounds, a reaction
CC       that is part of a thiamine salvage pathway. Thus, catalyzes the
CC       conversion of 4-amino-5-aminomethyl-2-methylpyrimidine to 4-amino-
CC       5-hydroxymethyl-2-methylpyrimidine (HMP).
CC       {ECO:0000256|PIRNR:PIRNR003170}.
CC   -!- CATALYTIC ACTIVITY: 4-amino-5-aminomethyl-2-methylpyrimidine +
CC       H(2)O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + ammonia.
CC       {ECO:0000256|PIRNR:PIRNR003170}.
CC   -!- CATALYTIC ACTIVITY: Thiamine + H(2)O = 4-amino-5-hydroxymethyl-2-
CC       methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole.
CC       {ECO:0000256|PIRNR:PIRNR003170}.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|PIRNR:PIRNR003170}.
CC   -!- SIMILARITY: Belongs to the TenA family.
CC       {ECO:0000256|PIRNR:PIRNR003170}.
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DR   EMBL; AP006627; BAD63208.1; -; Genomic_DNA.
DR   RefSeq; WP_011245524.1; NC_006582.1.
DR   ProteinModelPortal; Q5WK97; -.
DR   STRING; 66692.ABC0669; -.
DR   EnsemblBacteria; BAD63208; BAD63208; ABC0669.
DR   KEGG; bcl:ABC0669; -.
DR   PATRIC; 18920600; VBIBacCla58185_0705.
DR   eggNOG; COG0819; LUCA.
DR   eggNOG; ENOG4105ETU; Bacteria.
DR   HOGENOM; HOG000225158; -.
DR   KO; K03707; -.
DR   OMA; MYSSEEF; -.
DR   OrthoDB; EOG6JMMXP; -.
DR   BioCyc; BCLA66692:GHMP-699-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001168; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001168};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR003170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001168};
KW   Thiamine biosynthesis {ECO:0000256|PIRNR:PIRNR003170}.
FT   DOMAIN        9    216       TENA_THI-4. {ECO:0000259|Pfam:PF03070}.
FT   ACT_SITE    207    207       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR003170-1}.
SQ   SEQUENCE   223 AA;  25276 MW;  7CA91599A8A534FB CRC64;
     MKFSERIRKN ADPIWQASHN HPFVQGIGHG TLELEAFQYY MCQDYKYLIE YARVIALGTV
     LAPDLETMSG FAKALDETLN SEMDLHRAYA KRLGITQEQL EQTVPGPVTL AYSSAMMAEA
     QKGSLAELIA AILPCAWSYY EIGTALAKIP GATEHEAYGE WVKMYSSPEF GAIADWLIAK
     LDELAAEKSE AELDRIETIF MNTSRYEYMF WDMAYKQENW PIG
//
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