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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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphoribosyl-ATP diphosphatase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-HAMAP
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
ProteomesiUP000007096: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107Phosphoribosyl-ATP pyrophosphatasePRO_1000135299Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi405532.BCB4264_A1465.

Structurei

3D structure databases

ProteinModelPortaliB7HHG7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-PH family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0140.
HOGENOMiHOG000220965.
KOiK01523.
OMAiREKICNK.
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.

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.
RefSeqiYP_002366194.1. NC_011725.1.

Genome annotation databases

EnsemblBacteriaiACK61594; ACK61594; BCB4264_A1465.
GeneIDi7099028.
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.
RefSeqiYP_002366194.1. NC_011725.1.

3D structure databases

ProteinModelPortaliB7HHG7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi405532.BCB4264_A1465.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACK61594; ACK61594; BCB4264_A1465.
GeneIDi7099028.
KEGGibcb:BCB4264_A1465.
PATRICi18874885. VBIBacCer117876_1351.

Phylogenomic databases

eggNOGiCOG0140.
HOGENOMiHOG000220965.
KOiK01523.
OMAiREKICNK.
OrthoDBiEOG6CGCMH.

Enzyme and pathway databases

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

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. "Genome sequence of Bacillus cereus B4264."
    Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B4264.

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: February 4, 2015
This is version 42 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

External Data

Dasty 3

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 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.