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Protein

Phosphoribosyl-AMP cyclohydrolase

Gene

hisI

Organism
Methanolobus psychrophilus R15
Status
Unreviewed-Annotation score: -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:

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 (hisG)
  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 HisF (hisF), 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 bindingi92Zinc; shared with dimeric partnerUniRule annotation1
Metal bindingi99Zinc; shared with dimeric partnerUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolaseUniRule annotationImported
Biological processAmino-acid biosynthesis, Histidine biosynthesisUniRule annotation
LigandMagnesiumUniRule annotation, Metal-bindingUniRule annotation, ZincUniRule annotation

Enzyme and pathway databases

BioCyciMPSY1094980:G1HBJ-1737-MONOMER
UniPathwayi
UPA00031;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
ORF Names:Mpsy_1858Imported
OrganismiMethanolobus psychrophilus R15Imported
Taxonomic identifieri1094980 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaStenosarchaea groupMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanolobus
Proteomesi
  • UP000000459 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 101PRA-CHInterPro annotationAdd BLAST74

Sequence similaritiesi

Belongs to the PRA-CH family.UniRule annotation

Phylogenomic databases

KOiK01496
OrthoDBiPOG093Z0H2W

Family and domain databases

Gene3Di3.10.20.400, 1 hit
HAMAPiMF_01021 HisI, 1 hit
InterProiView protein in InterPro
IPR026660 PRA-CH
IPR002496 PRib_AMP_CycHydrolase_dom
IPR038019 PRib_AMP_CycHydrolase_sf
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
SUPFAMiSSF141734 SSF141734, 1 hit

Sequencei

Sequence statusi: Complete.

K4MFH8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MINIDDLKYE NGLIQAIAQD HTTKEVLMCA FMNKEALQKT METGIAHYWS
60 70 80 90 100
RSRGKLWKKG ESSGHMQKVK EMFIDCDMDA VLILVEQEGG ACHTGYRSCF
110 120
YRNMEGEVTG EKVFEPDDVY
Length:120
Mass (Da):13,765
Last modified:January 9, 2013 - v1
Checksum:i638DD866A5D5BEC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003083 Genomic DNA Translation: AFV24064.1
RefSeqiWP_015053772.1, NC_018876.1

Genome annotation databases

EnsemblBacteriaiAFV24064; AFV24064; Mpsy_1858
GeneIDi13845398
KEGGimpy:Mpsy_1858
PATRICifig|1094980.5.peg.1757

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003083 Genomic DNA Translation: AFV24064.1
RefSeqiWP_015053772.1, NC_018876.1

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFV24064; AFV24064; Mpsy_1858
GeneIDi13845398
KEGGimpy:Mpsy_1858
PATRICifig|1094980.5.peg.1757

Phylogenomic databases

KOiK01496
OrthoDBiPOG093Z0H2W

Enzyme and pathway databases

UniPathwayi
UPA00031;UER00008

BioCyciMPSY1094980:G1HBJ-1737-MONOMER

Family and domain databases

Gene3Di3.10.20.400, 1 hit
HAMAPiMF_01021 HisI, 1 hit
InterProiView protein in InterPro
IPR026660 PRA-CH
IPR002496 PRib_AMP_CycHydrolase_dom
IPR038019 PRib_AMP_CycHydrolase_sf
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
SUPFAMiSSF141734 SSF141734, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiK4MFH8_9EURY
AccessioniPrimary (citable) accession number: K4MFH8
Entry historyiIntegrated into UniProtKB/TrEMBL: January 9, 2013
Last sequence update: January 9, 2013
Last modified: October 10, 2018
This is version 30 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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