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Protein

Purine nucleoside phosphoramidase

Gene

hinT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes purine nucleotide phosphoramidates, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate), guanosine 5'monophosphomorpholidate (GMP-morpholidate) and tryptamine 5'guanosine monophosphate (TpGd) (PubMed:15703176, PubMed:20934431). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine--tRNA ligase, and lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) (PubMed:15703176). Is essential for the activity of the enzyme D-alanine dehydrogenase (DadA) and is required for E.coli to grow on D-alanine as a sole carbon source (PubMed:21754980). Is also required for growth at high salt concentrations (PubMed:15703176).3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881Purine nucleotide phosphoramidate1 Publication
Active sitei101 – 1011Tele-AMP-histidine intermediate2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 323Purine nucleotide phosphoramidate1 Publication
Nucleotide bindingi96 – 972Purine nucleotide phosphoramidate1 Publication
Nucleotide bindingi101 – 1033Purine nucleotide phosphoramidate1 Publication

GO - Molecular functioni

  • adenosine 5'-monophosphoramidase activity Source: EcoCyc
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  • D-alanine catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12172-MONOMER.
ECOL316407:JW1089-MONOMER.
MetaCyc:EG12172-MONOMER.
SABIO-RKP0ACE7.

Names & Taxonomyi

Protein namesi
Recommended name:
Purine nucleoside phosphoramidase1 Publication (EC:3.9.1.-3 Publications)
Alternative name(s):
Histidine triad nucleotide binding protein HinT
Short name:
HIT protein
Gene namesi
Name:hinT1 Publication
Synonyms:ycfF
Ordered Locus Names:b1103, JW1089
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12172. hinT.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene fail to grow on both D and L isomers of alanine due to a defect in DadA dehydrogenase activity, preventing D-alanine utilization (PubMed:21754980). The mutant cells do not have appreciable nucleoside phosphoramidase activity (PubMed:21754980, PubMed:15703176). The loss of hinT results in failure to grow in media containing 0.75 M KCl, 0.9 M NaCl, 0.5 M NaOAc, or 10 mM MnCl2 (PubMed:15703176).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011H → A or G: Abolishes enzyme activity. 3 Publications
Mutagenesisi114 – 1196Missing : Strongly reduces enzyme activity. 1 Publication
Mutagenesisi117 – 1193Missing : Abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 119119Purine nucleoside phosphoramidasePRO_0000109830Add
BLAST

Proteomic databases

EPDiP0ACE7.
PaxDbiP0ACE7.
PRIDEiP0ACE7.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi4261963. 7 interactions.
DIPiDIP-48009N.
IntActiP0ACE7. 14 interactions.
MINTiMINT-1266101.
STRINGi511145.b1103.

Structurei

Secondary structure

1
119
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 116Combined sources
Beta strandi19 – 224Combined sources
Beta strandi24 – 307Combined sources
Beta strandi35 – 4612Combined sources
Helixi51 – 533Combined sources
Helixi56 – 583Combined sources
Helixi59 – 7517Combined sources
Turni79 – 813Combined sources
Beta strandi83 – 897Combined sources
Helixi90 – 934Combined sources
Beta strandi97 – 993Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi113 – 1153Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N1SX-ray1.45A/B/E/F/I/J/M/N1-119[»]
3N1TX-ray1.72A/B/E/F1-119[»]
ProteinModelPortaliP0ACE7.
SMRiP0ACE7. Positions 1-119.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACE7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 115110HITPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi99 – 1057Histidine triad motif1 Publication

Sequence similaritiesi

Belongs to the HINT family.Curated
Contains 1 HIT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105K59. Bacteria.
COG0537. LUCA.
HOGENOMiHOG000061064.
InParanoidiP0ACE7.
KOiK02503.
OMAiIPTTNDV.
OrthoDBiEOG69GZSV.
PhylomeDBiP0ACE7.

Family and domain databases

Gene3Di3.30.428.10. 1 hit.
InterProiIPR019808. Histidine_triad_CS.
IPR001310. Histidine_triad_HIT.
IPR011146. HIT-like.
[Graphical view]
PANTHERiPTHR23089. PTHR23089. 1 hit.
PfamiPF01230. HIT. 1 hit.
[Graphical view]
PRINTSiPR00332. HISTRIAD.
SUPFAMiSSF54197. SSF54197. 1 hit.
PROSITEiPS00892. HIT_1. 1 hit.
PS51084. HIT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ACE7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEETIFSKI IRREIPSDIV YQDDLVTAFR DISPQAPTHI LIIPNILIPT
60 70 80 90 100
VNDVSAEHEQ ALGRMITVAA KIAEQEGIAE DGYRLIMNTN RHGGQEVYHI
110
HMHLLGGRPL GPMLAHKGL
Length:119
Mass (Da):13,241
Last modified:November 22, 2005 - v1
Checksum:iF0E6AAF177DC820B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74187.1.
AP009048 Genomic DNA. Translation: BAA35910.1.
X17615 Genomic DNA. No translation available.
PIRiJC5685.
RefSeqiNP_415621.3. NC_000913.3.
WP_000807125.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74187; AAC74187; b1103.
BAA35910; BAA35910; BAA35910.
GeneIDi948549.
KEGGiecj:JW1089.
eco:b1103.
PATRICi32117449. VBIEscCol129921_1147.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74187.1.
AP009048 Genomic DNA. Translation: BAA35910.1.
X17615 Genomic DNA. No translation available.
PIRiJC5685.
RefSeqiNP_415621.3. NC_000913.3.
WP_000807125.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N1SX-ray1.45A/B/E/F/I/J/M/N1-119[»]
3N1TX-ray1.72A/B/E/F1-119[»]
ProteinModelPortaliP0ACE7.
SMRiP0ACE7. Positions 1-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261963. 7 interactions.
DIPiDIP-48009N.
IntActiP0ACE7. 14 interactions.
MINTiMINT-1266101.
STRINGi511145.b1103.

Proteomic databases

EPDiP0ACE7.
PaxDbiP0ACE7.
PRIDEiP0ACE7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74187; AAC74187; b1103.
BAA35910; BAA35910; BAA35910.
GeneIDi948549.
KEGGiecj:JW1089.
eco:b1103.
PATRICi32117449. VBIEscCol129921_1147.

Organism-specific databases

EchoBASEiEB2090.
EcoGeneiEG12172. hinT.

Phylogenomic databases

eggNOGiENOG4105K59. Bacteria.
COG0537. LUCA.
HOGENOMiHOG000061064.
InParanoidiP0ACE7.
KOiK02503.
OMAiIPTTNDV.
OrthoDBiEOG69GZSV.
PhylomeDBiP0ACE7.

Enzyme and pathway databases

BioCyciEcoCyc:EG12172-MONOMER.
ECOL316407:JW1089-MONOMER.
MetaCyc:EG12172-MONOMER.
SABIO-RKP0ACE7.

Miscellaneous databases

EvolutionaryTraceiP0ACE7.
PROiP0ACE7.

Family and domain databases

Gene3Di3.30.428.10. 1 hit.
InterProiIPR019808. Histidine_triad_CS.
IPR001310. Histidine_triad_HIT.
IPR011146. HIT-like.
[Graphical view]
PANTHERiPTHR23089. PTHR23089. 1 hit.
PfamiPF01230. HIT. 1 hit.
[Graphical view]
PRINTSiPR00332. HISTRIAD.
SUPFAMiSSF54197. SSF54197. 1 hit.
PROSITEiPS00892. HIT_1. 1 hit.
PS51084. HIT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Sequence of the fhuE outer-membrane receptor gene of Escherichia coli K12 and properties of mutants."
    Sauer U., Hantke K., Braun V.
    Mol. Microbiol. 4:427-437(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
    Strain: K12.
  5. Baum B.
    Unpublished observations (MAR-1994)
    Cited for: IDENTIFICATION.
  6. "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."
    Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.
    Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: B / BL21.
  7. "31P NMR and genetic analysis establish hinT as the only Escherchia coli purine nucleoside phosphoramidase and as essential for growth under high salt conditions."
    Chou T.F., Bieganowski P., Shilinski K., Cheng J., Brenner C., Wagner C.R.
    J. Biol. Chem. 280:15356-15361(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF HIS-101, DISRUPTION PHENOTYPE.
  8. "E. coli histidine triad nucleotide binding protein 1 (ecHinT) is a catalytic regulator of D-alanine dehydrogenase (DadA) activity in vivo."
    Bardaweel S., Ghosh B., Chou T.F., Sadowsky M.J., Wagner C.R.
    PLoS ONE 6:E20897-E20897(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-101, DISRUPTION PHENOTYPE.
    Strain: K12 / BW25113.
  9. "Probing the impact of the echinT C-terminal domain on structure and catalysis."
    Bardaweel S., Pace J., Chou T.F., Cody V., Wagner C.R.
    J. Mol. Biol. 404:627-638(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH GMP, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF HIS-101; 114-LEU--LEU-119 AND 117-LYS--LEU-119.

Entry informationi

Entry nameiHINT_ECOLI
AccessioniPrimary (citable) accession number: P0ACE7
Secondary accession number(s): P36950, P75945
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: May 11, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.