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Q62GE7 (HIS2_BURMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. 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:BMA2706
OrganismBurkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]
Taxonomic identifier13373 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length122 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 – 122122Phosphoribosyl-ATP pyrophosphatase HAMAP MF_01020
PRO_0000230170

Sequences

Sequence LengthMass (Da)Tools
Q62GE7 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 3D2605F29B527D08

FASTA12213,361
        10         20         30         40         50         60 
MTQSTTEDTL LRLAAVIDSR KGGDPEQSYV SRLFHKGDDA ILKKIGEEAT EVVLAAKDVR 

        70         80         90        100        110        120 
QGGAPSALVG EVADLWFHCL VALSHFDLSP ADVIAELERR EGMSGIEEKA LRKRREREEN 


GG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000010 Genomic DNA. Translation: AAU48275.1.
RefSeqYP_104227.1. NC_006348.1.

3D structure databases

ProteinModelPortalQ62GE7.
SMRQ62GE7. Positions 8-102.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3091107.
GenomeReviewsGene locus BMA2706 in contig CP000010_GR.
KEGGbma:BMA2706.
PATRIC19120565. VBIBurMal55007_2776.
TIGRBMA2706.

Phylogenomic databases

HOGENOMHBG646527.
OMAETVMAAK.
ProtClustDBPRK00400.

Enzyme and pathway databases

BioCycBMAL243160:BMA_2706-MONOMER.

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_BURMA
AccessionPrimary (citable) accession number: Q62GE7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 41 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

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