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Protein

Phosphoribosyl-AMP cyclohydrolase

Gene

hisI

Organism
Bordetella avium (strain 197N)
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), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC), 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 bindingi80MagnesiumUniRule annotation1
Metal bindingi81Zinc; shared with dimeric partnerUniRule annotation1
Metal bindingi82MagnesiumUniRule annotation1
Metal bindingi84MagnesiumUniRule annotation1
Metal bindingi98Zinc; shared with dimeric partnerUniRule annotation1
Metal bindingi105Zinc; 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

BioCyciBAVI360910:GCKI-3354-MONOMER.
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:BAV3320
OrganismiBordetella avium (strain 197N)
Taxonomic identifieri360910 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
Proteomesi
  • UP000001977 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000633901 – 134Phosphoribosyl-AMP cyclohydrolaseAdd BLAST134

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi360910.BAV3320.

Structurei

3D structure databases

ProteinModelPortaliQ2KTT0.
SMRiQ2KTT0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-CH family.UniRule annotation

Phylogenomic databases

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

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.

Q2KTT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTEPDWMAD VVFDADGLIP AIAQDAENGQ ILMVAWMNRE SLAETAATGR
60 70 80 90 100
AVYWSRSRKK LWRKGEESGH AQQVHELRLD CDGDVILLKV HQNGGIACHT
110 120 130
GRASCFYRRL DGTSQRAAWV TVDPVLKDPE LIYK
Length:134
Mass (Da):15,013
Last modified:March 7, 2006 - v1
Checksum:i4D5DACC40E478E89
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM167904 Genomic DNA. Translation: CAJ50930.1.
RefSeqiWP_012418957.1. NC_010645.1.

Genome annotation databases

EnsemblBacteriaiCAJ50930; CAJ50930; BAV3320.
KEGGibav:BAV3320.

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_BORA1
AccessioniPrimary (citable) accession number: Q2KTT0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 7, 2006
Last modified: June 7, 2017
This is version 71 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