HINT_SHIFL
ID HINT_SHIFL Reviewed; 119 AA.
AC P0ACE9; P36950; P75945;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=SF1107, S1187;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42725.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP16613.1; -; Genomic_DNA.
DR RefSeq; NP_707018.2; NC_004337.2.
DR RefSeq; WP_000807125.1; NZ_UIQL01000002.1.
DR AlphaFoldDB; P0ACE9; -.
DR SMR; P0ACE9; -.
DR STRING; 198214.SF1107; -.
DR PRIDE; P0ACE9; -.
DR EnsemblBacteria; AAN42725; AAN42725; SF1107.
DR EnsemblBacteria; AAP16613; AAP16613; S1187.
DR GeneID; 1024069; -.
DR GeneID; 67414296; -.
DR KEGG; sfl:SF1107; -.
DR KEGG; sfx:S1187; -.
DR PATRIC; fig|198214.7.peg.1297; -.
DR HOGENOM; CLU_056776_8_1_6; -.
DR OMA; SDCLFCK; -.
DR OrthoDB; 1934382at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000109832"
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
