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Protein

Phosphoribosyl-ATP pyrophosphatase

Gene

hisE

Organism
Bacillus cereus (strain B4264)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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 (hisC), 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

BioCyciBCER405532:GI1K-1456-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:BCB4264_A1465
OrganismiBacillus cereus (strain B4264)
Taxonomic identifieri405532 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000007096 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 – 107107Phosphoribosyl-ATP pyrophosphatasePRO_1000135299Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB7HHG7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-PH family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000220965.
KOiK01523.
OMAiCSEVIIA.

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.

B7HHG7-1 [UniParc]FASTAAdd to basket

« Hide

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

RREIDTL
Length:107
Mass (Da):12,518
Last modified:February 10, 2009 - v1
Checksum:i97D18BBF614C5114
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001176 Genomic DNA. Translation: ACK61594.1.
RefSeqiWP_000426355.1. NC_011725.1.

Genome annotation databases

EnsemblBacteriaiACK61594; ACK61594; BCB4264_A1465.
KEGGibcb:BCB4264_A1465.
PATRICi18874885. VBIBacCer117876_1351.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001176 Genomic DNA. Translation: ACK61594.1.
RefSeqiWP_000426355.1. NC_011725.1.

3D structure databases

ProteinModelPortaliB7HHG7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACK61594; ACK61594; BCB4264_A1465.
KEGGibcb:BCB4264_A1465.
PATRICi18874885. VBIBacCer117876_1351.

Phylogenomic databases

HOGENOMiHOG000220965.
KOiK01523.
OMAiCSEVIIA.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00007.
BioCyciBCER405532:GI1K-1456-MONOMER.

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_BACC4
AccessioniPrimary (citable) accession number: B7HHG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: September 7, 2016
This is version 49 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

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.