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Q43925 (HIS3_AZOCH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 2, 2010. Version 52. 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-AMP cyclohydrolase

Short name=PRA-CH
EC=3.5.4.19
Gene names
Name:hisI
OrganismAzotobacter chroococcum mcd 1
Taxonomic identifier355 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length133 AA.
Sequence statusComplete.
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 HAMAP MF_01021.

Sequence similarities

Belongs to the PRA-CH family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionphosphoribosyl-AMP cyclohydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 133133Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01021
PRO_0000136457

Sequences

Sequence LengthMass (Da)Tools
Q43925 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: CEC538C94BE5EA34

FASTA13315,416
        10         20         30         40         50         60 
MKDWLDEIHW NADGLVPAIA QDHKTGRILM MAWMNRESLA LTVRENRAIY WSRSRGKLWR 

        70         80         90        100        110        120 
KGEESGHLQK VHEVRLDCDA DVIVLQVEQL GGIACHTGRE SCFYRVFEDG AWKVVEPILK 

       130 
DPDAIYHAGH RHE 

« Hide

References

[1]Yates M., Souza E.M.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U48404 Genomic DNA. Translation: AAA92106.1.

3D structure databases

ProteinModelPortalQ43925.
SMRQ43925. Positions 7-122.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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

Entry information

Entry nameHIS3_AZOCH
AccessionPrimary (citable) accession number: Q43925
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 2, 2010
This is version 52 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