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Q2N8I9 (HIS2_ERYLH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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:ELI_09550
OrganismErythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]
Taxonomic identifier314225 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesErythrobacteraceaeErythrobacter

Protein attributes

Sequence length104 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 – 104104Phosphoribosyl-ATP pyrophosphatase HAMAP MF_01020
PRO_0000319646

Sequences

Sequence LengthMass (Da)Tools
Q2N8I9 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 81476E1A819B463E

FASTA10411,174
        10         20         30         40         50         60 
MNTLQRLEAT IAARRNADPD SSYVARLNAK GLPKMAEKVG EEATETVIAA LTGSDEELVG 

        70         80         90        100 
EGADLIFHLL VLLQARGVSL DQVLAELDRR EGLSGLDEKA KRGD 

« Hide

References

[1]"Complete genome sequence of Erythrobacter litoralis HTCC2594."
Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.
J. Bacteriol. 191:2419-2420(2009) [PubMed: 19168610] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTCC2594.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000157 Genomic DNA. Translation: ABC64002.1.
RefSeqYP_458799.1. NC_007722.1.

3D structure databases

ProteinModelPortalQ2N8I9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2N8I9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3869493.
GenomeReviewsGene locus ELI_09550 in contig CP000157_GR.
KEGGeli:ELI_09550.
NMPDRfig|314225.3.peg.1129.
PATRIC21860938. VBIEryLit102657_1891.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0140.
HOGENOMHBG646527.
OMAETVMAAK.
ProtClustDBPRK00400.

Enzyme and pathway databases

BioCycELIT314225:ELI_09550-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_ERYLH
AccessionPrimary (citable) accession number: Q2N8I9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 7, 2006
Last modified: January 25, 2012
This is version 39 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