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Reviewed, UniProtKB/Swiss-Prot A5I248 (HIS2_CLOBH)

Last modified November 3, 2009. Version 19. 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: CBO1574
OrganismClostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier441771 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length110 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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 – 110110Phosphoribosyl-ATP pyrophosphatase HAMAP MF_01020
PRO_1000063336

Sequences

Sequence LengthMass (Da)Tools
A5I248-1 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 5D4F7F92B56333B3

FASTA11013,029
        10         20         30         40         50         60 
MNRNNVIDSL FNIIEDRKDK PIEGSYTGYL FEKGLDKILK KVGEESSEVI IAAKNEDEEE 

        70         80         90        100        110 
LIKEICDLTY HIMVLMVEKQ IKLDDIEKEL EKRRERICNK KNERKTIEKL 

« Hide

Cross-references

Sequence databases

AM412317 Genomic DNA. Translation: CAL83113.1.
RefSeqYP_001254081.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5185829.
GenomeReviewsGene locus CBO1574 in contig AM412317_GR.
KEGGcbo:CBO1574.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMACEKIGEE.

Family and domain databases

HAMAPMF_01020.
[Tree]
InterProIPR008179. PRib-ATP_pyrophosphohydrolase.
[Graphical view]
PfamPF01503. PRA-PH. 1 hit.
[Graphical view]
ProDomPD002611. Pra_PH/CH. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03188. histidine_hisI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS2_CLOBH
AccessionPrimary (citable) accession number: A5I248
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 26, 2007
Last modified: November 3, 2009
This is version 19 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