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Protein

Phosphoribosyl-AMP cyclohydrolase

Gene

hisI

Organism
Desulfotalea psychrophila (strain LSv54 / DSM 12343)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.UniRule annotation

Catalytic activityi

1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation
  • Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi: L-histidine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG)
  2. no protein annotated in this organism
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. no protein annotated in this organism
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi75MagnesiumUniRule annotation1
Metal bindingi76Zinc; shared with dimeric partnerUniRule annotation1
Metal bindingi77MagnesiumUniRule annotation1
Metal bindingi79MagnesiumUniRule annotation1
Metal bindingi93Zinc; shared with dimeric partnerUniRule annotation1
Metal bindingi100Zinc; shared with dimeric partnerUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00031; UER00008.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosyl-AMP cyclohydrolaseUniRule annotation (EC:3.5.4.19UniRule annotation)
Short name:
PRA-CHUniRule annotation
Gene namesi
Name:hisIUniRule annotation
Ordered Locus Names:DP2639
OrganismiDesulfotalea psychrophila (strain LSv54 / DSM 12343)
Taxonomic identifieri177439 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobulbaceaeDesulfotalea
Proteomesi
  • UP000000602 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002298201 – 127Phosphoribosyl-AMP cyclohydrolaseAdd BLAST127

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi177439.DP2639.

Structurei

3D structure databases

SMRiQ6AJV8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-CH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105K8F. Bacteria.
COG0139. LUCA.
HOGENOMiHOG000277504.
KOiK01496.
OMAiTGYRSCF.
OrthoDBiPOG091H050E.

Family and domain databases

HAMAPiMF_01021. HisI. 1 hit.
InterProiView protein in InterPro
IPR026660. PRA-CH.
IPR002496. PRib_AMP_CycHydrolase_dom.
PfamiView protein in Pfam
PF01502. PRA-CH. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002610. PRA_CycHdrlase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6AJV8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVELNFEKSV DGLLPAVVQD YVSGEVLMLA YINKLSWEKT LETGQAHYWS
60 70 80 90 100
RSRNSLWLKG ESSGNVQVIH DILVDCDSDT VVFKVDQIGD AACHTGHRSC
110 120
FFRRVHQGEL VVEGKPLFDP AQVYGSK
Length:127
Mass (Da):14,242
Last modified:September 13, 2004 - v1
Checksum:iFF7F1355EA9B52F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR522870 Genomic DNA. Translation: CAG37368.1.
RefSeqiWP_011189880.1. NC_006138.1.

Genome annotation databases

EnsemblBacteriaiCAG37368; CAG37368; DP2639.
KEGGidps:DP2639.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiHIS3_DESPS
AccessioniPrimary (citable) accession number: Q6AJV8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: September 13, 2004
Last modified: June 7, 2017
This is version 73 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families