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Reviewed, UniProtKB/Swiss-Prot Q7VSY4 (HIS2_BORPE)

Last modified February 9, 2010. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoribosyl-ATP pyrophosphatase
      Short name=PRA-PH
    EC=3.6.1.31
Gene names
Name: hisE
Ordered Locus Names: BP3775
OrganismBordetella pertussis [Complete proteome] [HAMAP]
Taxonomic identifier520 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length115 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate. HAMAP MF_01020

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP MF_01020

Subcellular location

Cytoplasm By similarity HAMAP MF_01020.

Sequence similarities

Belongs to the PRA-PH family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processhistidine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoribosyl-ATP diphosphatase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 115115Phosphoribosyl-ATP pyrophosphatase HAMAP MF_01020
PRO_0000136349

Sequences

Sequence LengthMass (Da)Tools
Q7VSY4-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: B4AB43E3F6332DCF

FASTA11512,631
        10         20         30         40         50         60 
MTTPTAGDDI LSRIADTLAT RRPEAGGDPQ SSYVAKLLSK APDAFLKKIG EEATELVMAA 

        70         80         90        100        110 
KDGQPDRIIS ETADLWFHCL VALTHYNLRP EDVLAELARR EGLSGLEEKA RRPRD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX640422 Genomic DNA. Translation: CAE44031.1.
RefSeqNP_882276.1.

3D structure databases

SMRQ7VSY4. Positions 9-102.
ModBaseSearch...

Genome annotation databases

GeneID2665061.
KEGGbpe:BP3775.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG646527.
OMAETVMAAK.

Enzyme and pathway databases

BioCycBPER257313:BP3775-MONOMER.
BRENDA3.6.1.31. 21511.

Family and domain databases

HAMAPMF_01020. HisE.
[Tree]
InterProIPR008179. PRib-ATP_pyrophosphohydrolase.
IPR021130. PRib-ATP_pyroPHydrolase-like.
[Graphical view]
PfamPF01503. PRA-PH. 1 hit.
[Graphical view]
TIGRFAMsTIGR03188. histidine_hisI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS2_BORPE
AccessionPrimary (citable) accession number: Q7VSY4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: October 1, 2003
Last modified: February 9, 2010
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents