ID   HINT_ECO57              Reviewed;         119 AA.
AC   P0ACE8; P36950; P75945;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Purine nucleoside phosphoramidase {ECO:0000250|UniProtKB:P0ACE7};
DE            EC=3.9.1.- {ECO:0000250|UniProtKB:P0ACE7};
DE   AltName: Full=Histidine triad nucleotide binding protein HinT;
DE            Short=HIT protein;
GN   Name=hinT; OrderedLocusNames=Z1742, ECs1481;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Hydrolyzes purine nucleotide phosphoramidates, including
CC       adenosine 5'monophosphoramidate (AMP-NH2), adenosine
CC       5'monophosphomorpholidate (AMP-morpholidate), guanosine
CC       5'monophosphomorpholidate (GMP-morpholidate) and tryptamine 5'guanosine
CC       monophosphate (TpGd). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-
CC       acetyl lysine methyl ester)) generated by lysine tRNA ligase and lysyl-
CC       GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)). Is essential
CC       for the activity of the enzyme D-alanine dehydrogenase (DadA).
CC       {ECO:0000250|UniProtKB:P0ACE7}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0ACE7}.
CC   -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG55849.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34904.1; -; Genomic_DNA.
DR   PIR; A99814; A99814.
DR   PIR; E85673; E85673.
DR   RefSeq; NP_309508.2; NC_002695.1.
DR   RefSeq; WP_000807125.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0ACE8; -.
DR   SMR; P0ACE8; -.
DR   STRING; 155864.EDL933_1681; -.
DR   EnsemblBacteria; AAG55849; AAG55849; Z1742.
DR   EnsemblBacteria; BAB34904; BAB34904; ECs_1481.
DR   GeneID; 67414296; -.
DR   GeneID; 912424; -.
DR   KEGG; ece:Z1742; -.
DR   KEGG; ecs:ECs_1481; -.
DR   PATRIC; fig|386585.9.peg.1582; -.
DR   eggNOG; COG0537; Bacteria.
DR   HOGENOM; CLU_056776_8_1_6; -.
DR   OMA; SDCLFCK; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.428.10; -; 1.
DR   InterPro; IPR019808; Histidine_triad_CS.
DR   InterPro; IPR001310; Histidine_triad_HIT.
DR   InterPro; IPR011146; HIT-like.
DR   InterPro; IPR036265; HIT-like_sf.
DR   PANTHER; PTHR23089; PTHR23089; 1.
DR   Pfam; PF01230; HIT; 1.
DR   PRINTS; PR00332; HISTRIAD.
DR   SUPFAM; SSF54197; SSF54197; 1.
DR   PROSITE; PS00892; HIT_1; 1.
DR   PROSITE; PS51084; HIT_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..119
FT                   /note="Purine nucleoside phosphoramidase"
FT                   /id="PRO_0000109831"
FT   DOMAIN          6..115
FT                   /note="HIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT   MOTIF           99..105
FT                   /note="Histidine triad motif"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACE7"
FT   ACT_SITE        101
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACE7"
FT   BINDING         30..32
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACE7"
FT   BINDING         88
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACE7"
FT   BINDING         96..97
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACE7"
FT   BINDING         101..103
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACE7"
SQ   SEQUENCE   119 AA;  13241 MW;  F0E6AAF177DC820B CRC64;
     MAEETIFSKI IRREIPSDIV YQDDLVTAFR DISPQAPTHI LIIPNILIPT VNDVSAEHEQ
     ALGRMITVAA KIAEQEGIAE DGYRLIMNTN RHGGQEVYHI HMHLLGGRPL GPMLAHKGL