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Protein

Phosphoribosyl-ATP pyrophosphatase

Gene

hisE

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
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 regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG)
  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 1 (hisC1), Histidinol-phosphate aminotransferase 2 (hisC2)
  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

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:BC_1412
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000001417 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001363451 – 107Phosphoribosyl-ATP pyrophosphataseAdd BLAST107

Proteomic databases

PRIDEiQ81G00.

Interactioni

Protein-protein interaction databases

STRINGi226900.BC1412.

Structurei

Secondary structure

1107
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 17Combined sources13
Helixi24 – 31Combined sources8
Helixi33 – 52Combined sources20
Helixi56 – 76Combined sources21
Helixi81 – 94Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YVWX-ray2.60A/B/C/D1-107[»]
ProteinModelPortaliQ81G00.
SMRiQ81G00.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ81G00.

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-PH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105KPZ. Bacteria.
COG0140. LUCA.
KOiK01523.
OMAiGDADKSY.

Family and domain databases

CDDicd11534. NTP-PPase_HisIE_like. 1 hit.
HAMAPiMF_01020. HisE. 1 hit.
InterProiIPR008179. HisE.
IPR021130. PRib-ATP_PPHydrolase-like.
[Graphical view]
PfamiPF01503. PRA-PH. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03188. histidine_hisI. 1 hit.

Sequencei

Sequence statusi: Complete.

Q81G00-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENAFKLLYK TIEERKGSPL PESYTNYLFS KGEDKILKKI GEECAEVIIA
60 70 80 90 100
CKNNDKEEVV KEMVDVFYHC FVLLAEKNIA LEDVMREVKE RNGKLSRVGD

RREIDTL
Length:107
Mass (Da):12,446
Last modified:June 1, 2003 - v1
Checksum:iA2B1899D636C7316
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP08393.1.
RefSeqiNP_831192.1. NC_004722.1.
WP_000426358.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP08393; AAP08393; BC_1412.
GeneIDi1203761.
KEGGibce:BC1412.
PATRICi32598560. VBIBacCer54481_1389.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP08393.1.
RefSeqiNP_831192.1. NC_004722.1.
WP_000426358.1. NC_004722.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YVWX-ray2.60A/B/C/D1-107[»]
ProteinModelPortaliQ81G00.
SMRiQ81G00.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC1412.

Proteomic databases

PRIDEiQ81G00.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP08393; AAP08393; BC_1412.
GeneIDi1203761.
KEGGibce:BC1412.
PATRICi32598560. VBIBacCer54481_1389.

Phylogenomic databases

eggNOGiENOG4105KPZ. Bacteria.
COG0140. LUCA.
KOiK01523.
OMAiGDADKSY.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00007.

Miscellaneous databases

EvolutionaryTraceiQ81G00.

Family and domain databases

CDDicd11534. NTP-PPase_HisIE_like. 1 hit.
HAMAPiMF_01020. HisE. 1 hit.
InterProiIPR008179. HisE.
IPR021130. PRib-ATP_PPHydrolase-like.
[Graphical view]
PfamiPF01503. PRA-PH. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03188. histidine_hisI. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHIS2_BACCR
AccessioniPrimary (citable) accession number: Q81G00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 96 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.