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Reviewed, UniProtKB/Swiss-Prot Q7N6I6 (HIS2_PHOLL)

Last modified June 16, 2009. Version 37. 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:
    Histidine biosynthesis bifunctional protein hisIE
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosyl-AMP cyclohydrolase
                Short name=PRA-CH
              EC=3.5.4.19
    2- Recommended name:
            Phosphoribosyl-ATP pyrophosphatase
                Short name=PRA-PH
              EC=3.6.1.31
Gene names
Name: hisI
Synonyms: hisIE
Ordered Locus Names: plu1564
OrganismPhotorhabdus luminescens subsp. laumondii [Complete proteome] [HAMAP]
Taxonomic identifier141679 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus

Protein attributes

Sequence length201 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_01019

1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP MF_01019

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP MF_01019

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

In the N-terminal section; belongs to the PRA-CH family.

In the C-terminal section; belongs to the PRA-PH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019
PRO_0000136421

Regions

Region1 – 114114Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
Region115 – 20187Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

Sequence LengthMass (Da)Tools
Q7N6I6-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: D6F71C699D6674BF

FASTA20122,615
        10         20         30         40         50         60 
MLTAQQIEKL DWEKVAYMMP VIVQHAISGD VLMMGYMNKE ALNITISSGK ITFFSRSKQR 

        70         80         90        100        110        120 
LWTKGESSGH FLNLVNIYPD CDNDTLLALA DPIGPTCHFG THSCFAPAQT EWGFLYQLEK 

       130        140        150        160        170        180 
LLASRKTADP DHSYTAKLYA SGTKRIAQKV GEEGLETALA AAVNNREELT NEAADLMYHL 

       190        200 
MVLLQDQELD LSCVIRRLRE R 

« Hide

Cross-references

Sequence databases

BX571864 Genomic DNA. Translation: CAE13857.1.
RefSeqNP_928855.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2801559.
GenomeReviewsGene locus plu1564 in contig BX470251_GR.
KEGGplu:plu1564.
NMPDRfig|243265.1.peg.1479.

Organism-specific databases

PhotoListplu1564.
CMRSearch...

Phylogenomic databases

HOGENOMQ7N6I6.
OMAQ7N6I6. VHYWSRS.

Enzyme and pathway databases

BioCycPLUM243265:PLU1564-MON.
BRENDA3.5.4.19. 308689.
3.6.1.31. 308689.

Family and domain databases

HAMAPMF_01019.
[Tree]
InterProIPR002496. PRA_CycHdrlase.
IPR008179. PRib-ATP_pyrophosphohydrolase.
[Graphical view]
PfamPF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
ProDomPD002610. PRA_cyclohydro. 1 hit.
PD002611. Pra_PH/CH. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03188. histidine_hisI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS2_PHOLL
AccessionPrimary (citable) accession number: Q7N6I6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: December 15, 2003
Last modified: June 16, 2009
This is version 37 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