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Protein

Phosphoribosyl-ATP pyrophosphatase

Gene

hisE

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate.UniRule annotation

Pathwayi: L-histidine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciCVIO243365:GHUD-631-MONOMER.
UniPathwayiUPA00031; UER00007.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosyl-ATP pyrophosphataseUniRule annotation (EC:3.6.1.31UniRule annotation)
Short name:
PRA-PHUniRule annotation
Gene namesi
Name:hisEUniRule annotation
Ordered Locus Names:CV_0621
OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Taxonomic identifieri243365 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
Proteomesi
  • UP000001424 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 108108Phosphoribosyl-ATP pyrophosphatasePRO_0000136356Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243365.CV_0621.

Structurei

Secondary structure

1
108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1510Combined sources
Helixi16 – 183Combined sources
Turni21 – 233Combined sources
Helixi25 – 328Combined sources
Helixi34 – 5320Combined sources
Helixi57 – 7721Combined sources
Helixi82 – 9211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A7WX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-108[»]
ProteinModelPortaliQ7P0E6.
SMRiQ7P0E6. Positions 4-94.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7P0E6.

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-PH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105KPZ. Bacteria.
COG0140. LUCA.
HOGENOMiHOG000220965.
KOiK01523.
OMAiEQSWTAK.
OrthoDBiEOG6CGCMH.

Family and domain databases

HAMAPiMF_01020. HisE.
InterProiIPR008179. PRib-ATP_PPHydrolase.
IPR021130. PRib-ATP_PPHydrolase-like.
[Graphical view]
PfamiPF01503. PRA-PH. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03188. histidine_hisI. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7P0E6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPDVLKNIA DTLEARREAA PQSSYVASLF HKGEDAILKK VAEEAAETLM
60 70 80 90 100
ASKDKDKLHL VREVADLWFH TMVLLTYHGL RPEDVVMELH RREGISGLDE

KASRKPTA
Length:108
Mass (Da):12,139
Last modified:December 15, 2003 - v1
Checksum:iF1A172FD0CA204D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016825 Genomic DNA. Translation: AAQ58297.1.
RefSeqiWP_011134176.1. NC_005085.1.

Genome annotation databases

EnsemblBacteriaiAAQ58297; AAQ58297; CV_0621.
GeneIDi24946820.
KEGGicvi:CV_0621.
PATRICi21436038. VBIChrVio67196_0620.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016825 Genomic DNA. Translation: AAQ58297.1.
RefSeqiWP_011134176.1. NC_005085.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A7WX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-108[»]
ProteinModelPortaliQ7P0E6.
SMRiQ7P0E6. Positions 4-94.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243365.CV_0621.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ58297; AAQ58297; CV_0621.
GeneIDi24946820.
KEGGicvi:CV_0621.
PATRICi21436038. VBIChrVio67196_0620.

Phylogenomic databases

eggNOGiENOG4105KPZ. Bacteria.
COG0140. LUCA.
HOGENOMiHOG000220965.
KOiK01523.
OMAiEQSWTAK.
OrthoDBiEOG6CGCMH.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00007.
BioCyciCVIO243365:GHUD-631-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ7P0E6.

Family and domain databases

HAMAPiMF_01020. HisE.
InterProiIPR008179. PRib-ATP_PPHydrolase.
IPR021130. PRib-ATP_PPHydrolase-like.
[Graphical view]
PfamiPF01503. PRA-PH. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03188. histidine_hisI. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
    Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A.
    , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
    Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Entry informationi

Entry nameiHIS2_CHRVO
AccessioniPrimary (citable) accession number: Q7P0E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: December 15, 2003
Last modified: November 11, 2015
This is version 91 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.