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Database: UniProt/TrEMBL
Entry: A6T987_KLEP7
LinkDB: A6T987_KLEP7
Original site: A6T987_KLEP7 
ID   A6T987_KLEP7            Unreviewed;       214 AA.
AC   A6T987;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   08-JUN-2016, entry version 48.
DE   RecName: Full=Aminopyrimidine aminohydrolase {ECO:0000256|PIRNR:PIRNR003170};
DE            EC=3.5.99.2 {ECO:0000256|PIRNR:PIRNR003170};
GN   ORFNames=KPN_01727 {ECO:0000313|EMBL:ABR77158.1};
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH
OS   78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR77158.1, ECO:0000313|Proteomes:UP000000265};
RN   [1] {ECO:0000313|EMBL:ABR77158.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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; CP000647; ABR77158.1; -; Genomic_DNA.
DR   RefSeq; WP_002904912.1; NC_009648.1.
DR   ProteinModelPortal; A6T987; -.
DR   STRING; 272620.KPN_01727; -.
DR   DNASU; 5341050; -.
DR   EnsemblBacteria; ABR77158; ABR77158; KPN_01727.
DR   KEGG; kpn:KPN_01727; -.
DR   PATRIC; 20457734; VBIKlePne13394_1755.
DR   eggNOG; ENOG4105JRH; Bacteria.
DR   eggNOG; COG0819; LUCA.
DR   HOGENOM; HOG000251146; -.
DR   KO; K03707; -.
DR   OMA; FAAEWMY; -.
DR   OrthoDB; EOG6JMMXP; -.
DR   BioCyc; KPNE272620:GKDC-1727-MONOMER; -.
DR   Proteomes; UP000000265; 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   Pfam; PF03070; TENA_THI-4; 1.
DR   PIRSF; PIRSF003170; Pet18p; 1.
DR   SUPFAM; SSF48613; SSF48613; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000265};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR003170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000265};
KW   Thiamine biosynthesis {ECO:0000256|PIRNR:PIRNR003170}.
FT   DOMAIN       10    213       TENA_THI-4. {ECO:0000259|Pfam:PF03070}.
FT   ACT_SITE    204    204       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR003170-1}.
SQ   SEQUENCE   214 AA;  25181 MW;  E6534FE8A6483B04 CRC64;
     MEAFSERLLR EHQPAWQAMQ QHPFVTDIEQ DRLPTVVFNR YLVFEGNFVA TAIAIFALGV
     SKAPGIQQQR WLIGVLNALV DIQIAWFEQV LSARQIDPAE YPDDLPGVRR FRDGMLRTAH
     EGSYEQIVTL MFGAEWMYYF WCRRASEHYQ SDADLRRWVE MHAEDEFYQQ ALWLKNELDR
     CAMALSEDEK QALSALYGEV LQWEIDFHHA AYEE
//
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