HINT_ECOLI
ID HINT_ECOLI Reviewed; 119 AA.
AC P0ACE7; P36950; P75945;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Purine nucleoside phosphoramidase {ECO:0000303|PubMed:15703176};
DE EC=3.9.1.- {ECO:0000269|PubMed:15703176, ECO:0000269|PubMed:20934431, ECO:0000269|PubMed:21754980};
DE AltName: Full=Histidine triad nucleotide binding protein HinT;
DE Short=HIT protein;
GN Name=hinT {ECO:0000303|PubMed:15703176}; Synonyms=ycfF;
GN OrderedLocusNames=b1103, JW1089;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RC STRAIN=K12;
RX PubMed=2162465; DOI=10.1111/j.1365-2958.1990.tb00609.x;
RA Sauer U., Hantke K., Braun V.;
RT "Sequence of the fhuE outer-membrane receptor gene of Escherichia coli K12
RT and properties of mutants.";
RL Mol. Microbiol. 4:427-437(1990).
RN [5]
RP IDENTIFICATION.
RA Baum B.;
RL Unpublished observations (MAR-1994).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [7]
RP CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF HIS-101,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=15703176; DOI=10.1074/jbc.m500434200;
RA Chou T.F., Bieganowski P., Shilinski K., Cheng J., Brenner C., Wagner C.R.;
RT "31P NMR and genetic analysis establish hinT as the only Escherchia coli
RT purine nucleoside phosphoramidase and as essential for growth under high
RT salt conditions.";
RL J. Biol. Chem. 280:15356-15361(2005).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-101, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=21754980; DOI=10.1371/journal.pone.0020897;
RA Bardaweel S., Ghosh B., Chou T.F., Sadowsky M.J., Wagner C.R.;
RT "E. coli histidine triad nucleotide binding protein 1 (ecHinT) is a
RT catalytic regulator of D-alanine dehydrogenase (DadA) activity in vivo.";
RL PLoS ONE 6:E20897-E20897(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH GMP, CATALYTIC
RP ACTIVITY, FUNCTION, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF HIS-101;
RP 114-LEU--LEU-119 AND 117-LYS--LEU-119.
RX PubMed=20934431; DOI=10.1016/j.jmb.2010.09.066;
RA Bardaweel S., Pace J., Chou T.F., Cody V., Wagner C.R.;
RT "Probing the impact of the echinT C-terminal domain on structure and
RT catalysis.";
RL J. Mol. Biol. 404:627-638(2010).
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) (PubMed:15703176, PubMed:20934431). Hydrolyzes
CC lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester))
CC generated by lysine--tRNA ligase, and lysyl-GMP (GMP-N-epsilon-(N-
CC alpha-acetyl lysine methyl ester)) (PubMed:15703176). Is essential for
CC the activity of the enzyme D-alanine dehydrogenase (DadA) and is
CC required for E.coli to grow on D-alanine as a sole carbon source
CC (PubMed:21754980). Is also required for growth at high salt
CC concentrations (PubMed:15703176). {ECO:0000269|PubMed:15703176,
CC ECO:0000269|PubMed:20934431, ECO:0000269|PubMed:21754980}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15703176,
CC ECO:0000269|PubMed:20934431}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow on both D
CC and L isomers of alanine due to a defect in DadA dehydrogenase
CC activity, preventing D-alanine utilization (PubMed:21754980). The
CC mutant cells do not have appreciable nucleoside phosphoramidase
CC activity (PubMed:21754980, PubMed:15703176). The loss of hinT results
CC in failure to grow in media containing 0.75 M KCl, 0.9 M NaCl, 0.5 M
CC NaOAc, or 10 mM MnCl(2) (PubMed:15703176).
CC {ECO:0000269|PubMed:15703176, ECO:0000269|PubMed:21754980}.
CC -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
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DR EMBL; U00096; AAC74187.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35910.1; -; Genomic_DNA.
DR EMBL; X17615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JC5685; JC5685.
DR RefSeq; NP_415621.3; NC_000913.3.
DR RefSeq; WP_000807125.1; NZ_STEB01000016.1.
DR PDB; 3N1S; X-ray; 1.45 A; A/B/E/F/I/J/M/N=1-119.
DR PDB; 3N1T; X-ray; 1.72 A; A/B/E/F=1-119.
DR PDBsum; 3N1S; -.
DR PDBsum; 3N1T; -.
DR AlphaFoldDB; P0ACE7; -.
DR SMR; P0ACE7; -.
DR BioGRID; 4261963; 16.
DR BioGRID; 852843; 1.
DR DIP; DIP-48009N; -.
DR IntAct; P0ACE7; 14.
DR STRING; 511145.b1103; -.
DR jPOST; P0ACE7; -.
DR PaxDb; P0ACE7; -.
DR PRIDE; P0ACE7; -.
DR EnsemblBacteria; AAC74187; AAC74187; b1103.
DR EnsemblBacteria; BAA35910; BAA35910; BAA35910.
DR GeneID; 67414296; -.
DR GeneID; 948549; -.
DR KEGG; ecj:JW1089; -.
DR KEGG; eco:b1103; -.
DR PATRIC; fig|1411691.4.peg.1164; -.
DR EchoBASE; EB2090; -.
DR eggNOG; COG0537; Bacteria.
DR HOGENOM; CLU_056776_8_1_6; -.
DR InParanoid; P0ACE7; -.
DR OMA; SDCLFCK; -.
DR PhylomeDB; P0ACE7; -.
DR BioCyc; EcoCyc:EG12172-MON; -.
DR BioCyc; MetaCyc:EG12172-MON; -.
DR SABIO-RK; P0ACE7; -.
DR EvolutionaryTrace; P0ACE7; -.
DR PRO; PR:P0ACE7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; IDA:EcoCyc.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0055130; P:D-alanine catabolic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..119
FT /note="Purine nucleoside phosphoramidase"
FT /id="PRO_0000109830"
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:0000305|PubMed:20934431"
FT ACT_SITE 101
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000269|PubMed:15703176,
FT ECO:0000269|PubMed:20934431"
FT BINDING 30..32
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|PubMed:20934431,
FT ECO:0007744|PDB:3N1S"
FT BINDING 88
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|PubMed:20934431,
FT ECO:0007744|PDB:3N1S"
FT BINDING 96..97
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|PubMed:20934431,
FT ECO:0007744|PDB:3N1S"
FT BINDING 101..103
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|PubMed:20934431,
FT ECO:0007744|PDB:3N1S"
FT MUTAGEN 101
FT /note="H->A,G: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:15703176,
FT ECO:0000269|PubMed:20934431, ECO:0000269|PubMed:21754980"
FT MUTAGEN 114..119
FT /note="Missing: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:20934431"
FT MUTAGEN 117..119
FT /note="Missing: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:20934431"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:3N1S"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:3N1S"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:3N1S"
FT STRAND 35..46
FT /evidence="ECO:0007829|PDB:3N1S"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3N1S"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3N1S"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:3N1S"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:3N1S"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:3N1S"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:3N1S"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3N1S"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:3N1S"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3N1S"
SQ SEQUENCE 119 AA; 13241 MW; F0E6AAF177DC820B CRC64;
MAEETIFSKI IRREIPSDIV YQDDLVTAFR DISPQAPTHI LIIPNILIPT VNDVSAEHEQ
ALGRMITVAA KIAEQEGIAE DGYRLIMNTN RHGGQEVYHI HMHLLGGRPL GPMLAHKGL
