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Reviewed, UniProtKB/Swiss-Prot Q4KJL5 (HIS31_PSEF5)

Last modified June 16, 2009. Version 22. 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-AMP cyclohydrolase 1
      Short name=PRA-CH 1
    EC=3.5.4.19
Gene names
Name: hisI1
Ordered Locus Names: PFL_0424
OrganismPseudomonas fluorescens (strain Pf-5 / ATCC BAA-477) [Complete proteome] [HAMAP]
Taxonomic identifier220664 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length130 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP MF_01021

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. HAMAP MF_01021

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the PRA-CH family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   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 functionphosphoribosyl-AMP cyclohydrolase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 130130Phosphoribosyl-AMP cyclohydrolase 1 HAMAP MF_01021
PRO_0000229834

Sequences

Sequence LengthMass (Da)Tools
Q4KJL5-1 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 90667CFECE9C6990

FASTA13015,006
        10         20         30         40         50         60 
MKDWLDQIKW DADGLVPAIA QDHKTGRVLM MAWMNREALS LTAAENRAIY WSRSRGKLWR 

        70         80         90        100        110        120 
KGEESGHVQK LHEMRLDCDA DVIILMVEQI GDIACHTGRH SCFYRVYEDG EWKTVEPVLK 

       130 
DPHAIYSAGH 

« Hide

Cross-references

Sequence databases

CP000076 Genomic DNA. Translation: AAY95833.1.
RefSeqYP_257568.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3481015.
GenomeReviewsGene locus PFL_0424 in contig CP000076_GR.
KEGGpfl:PFL_0424.
NMPDRfig|220664.3.peg.1906.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ4KJL5.
OMAQ4KJL5. LWLKGES.

Enzyme and pathway databases

BioCycPFLU220664:PFL_0424-MON.

Family and domain databases

HAMAPMF_01021.
[Tree]
InterProIPR002496. PRA_CycHdrlase.
[Graphical view]
PfamPF01502. PRA-CH. 1 hit.
[Graphical view]
ProDomPD002610. PRA_cyclohydro. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameHIS31_PSEF5
AccessionPrimary (citable) accession number: Q4KJL5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: August 2, 2005
Last modified: June 16, 2009
This is version 22 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