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A5VT44 (HIS2_BRUO2) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BOV_2006
OrganismBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [Complete proteome] [HAMAP]
Taxonomic identifier444178 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length107 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: UniProtKB-KW

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 107107Phosphoribosyl-ATP pyrophosphatase HAMAP MF_01020
PRO_1000063323

Sequences

Sequence LengthMass (Da)Tools
A5VT44 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 4335A80E49ACB391

FASTA10711,253
        10         20         30         40         50         60 
MSQFTLADLE RIVAERASVT DGTSYTASLV AKGQPKAAQK LGEEAVETVI AAVSGDRAGV 

        70         80         90        100 
VSESADLLYH LAVVWNIAGV ALEDVLQELQ RRTAQTGLAE KASRPKG 

« Hide

References

[1]Paulsen I.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25840 / 63/290 / NCTC 10512.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000708 Genomic DNA. Translation: ABQ61505.1.
RefSeqYP_001259891.1. NC_009505.1.

3D structure databases

ProteinModelPortalA5VT44.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5VT44.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5202646.
GenomeReviewsGene locus BOV_2006 in contig CP000708_GR.
KEGGbov:BOV_2006.
PATRIC17864152. VBIBruOvi136990_3447.
TIGRBOV_2006.

Phylogenomic databases

HOGENOMHBG646527.
OMAETVMAAK.
ProtClustDBPRK00400.

Family and domain databases

HAMAPMF_01020. HisE.
[Tree]
InterProIPR008179. PRib-ATP_PPHydrolase.
IPR021130. PRib-ATP_PPHydrolase-like.
[Graphical view]
KOK01523.
PfamPF01503. PRA-PH. 1 hit.
[Graphical view]
TIGRFAMsTIGR03188. Histidine_hisI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS2_BRUO2
AccessionPrimary (citable) accession number: A5VT44
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families