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Protein

Phosphoribosyl-AMP cyclohydrolase

Gene

hisI

Organism
Brucella suis biovar 1 (strain 1330)
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 regulatory subunit (hisZ), 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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  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 bindingi91MagnesiumUniRule annotation1
Metal bindingi92Zinc; shared with dimeric partnerUniRule annotation1
Metal bindingi93MagnesiumUniRule annotation1
Metal bindingi95MagnesiumUniRule annotation1
Metal bindingi110Zinc; shared with dimeric partnerUniRule annotation1
Metal bindingi117Zinc; 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:BR1076, BS1330_I1072
OrganismiBrucella suis biovar 1 (strain 1330)
Taxonomic identifieri204722 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000007104 Componenti: Chromosome I

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001364671 – 139Phosphoribosyl-AMP cyclohydrolaseAdd BLAST139

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ8G0L3.
SMRiQ8G0L3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-CH family.UniRule annotation

Phylogenomic databases

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.

Q8G0L3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIFPAQPSD KKAVEEGAAF MPRFDASGLI TAIVTDARDG ELLMVAHMNE
60 70 80 90 100
EALRLTLETG IAHYWSRSRK TLWKKGETSG NLQSVVELRT DCDQDALWLK
110 120 130
VHVAGDGPTC HTGRRSCFYR QVVSSGGKVA LTMVSDHDQ
Length:139
Mass (Da):15,308
Last modified:November 7, 2003 - v2
Checksum:iA150156774661556
GO

Sequence cautioni

The sequence AAN29996 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014291 Genomic DNA. Translation: AAN29996.1. Different initiation.
CP002997 Genomic DNA. Translation: AEM18414.1.
RefSeqiWP_004690855.1. NZ_KN046804.1.

Genome annotation databases

EnsemblBacteriaiAAN29996; AAN29996; BR1076.
AEM18414; AEM18414; BS1330_I1072.
KEGGibms:BR1076.
bsi:BS1330_I1072.
PATRICifig|204722.21.peg.3681.

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_BRUSU
AccessioniPrimary (citable) accession number: Q8G0L3
Secondary accession number(s): G0K9Z8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 7, 2003
Last modified: June 7, 2017
This is version 89 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Brucella suis
    Brucella suis (strain 1330): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families