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Protein

Phosphoribosyl-AMP cyclohydrolase

Gene

hisI

Organism
Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
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 HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC-1), Histidinol-phosphate aminotransferase (hisC-2)
  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 bindingi92MagnesiumUniRule annotation1
Metal bindingi93Zinc; shared with dimeric partnerUniRule annotation1
Metal bindingi94MagnesiumUniRule annotation1
Metal bindingi96MagnesiumUniRule annotation1
Metal bindingi109Zinc; shared with dimeric partnerUniRule annotation1
Metal bindingi116Zinc; shared with dimeric partnerUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Magnesium, 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:ABO_2134
OrganismiAlcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
Taxonomic identifieri393595 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesAlcanivoracaceaeAlcanivorax
Proteomesi
  • UP000008871 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003196801 – 142Phosphoribosyl-AMP cyclohydrolaseAdd BLAST142

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi393595.ABO_2134.

Structurei

3D structure databases

ProteinModelPortaliQ0VML6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-CH family.UniRule annotation

Phylogenomic databases

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

Family and domain databases

HAMAPiMF_01021. HisI. 1 hit.
InterProiIPR026660. PRA-CH.
IPR002496. PRib_AMP_CycHydrolase_dom.
[Graphical view]
PfamiPF01502. PRA-CH. 1 hit.
[Graphical view]
ProDomiPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Q0VML6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKHNEQQPE GFQISLKEAL DNLAFNDAGL VAAIAQQHDS GEVLMMAWMN
60 70 80 90 100
REAIEETLAT GRVCYFSRSR GKLWRKGESS GQVQTLKELR IDCDGDALLV
110 120 130 140
KVDQTGSACH TGRRDCFYWK ADANNVTIDK APIKDPKELY GK
Length:142
Mass (Da):15,938
Last modified:September 5, 2006 - v1
Checksum:i1AB3214F6B1C4E9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM286690 Genomic DNA. Translation: CAL17582.1.
RefSeqiWP_011589412.1. NC_008260.1.

Genome annotation databases

EnsemblBacteriaiCAL17582; CAL17582; ABO_2134.
KEGGiabo:ABO_2134.
PATRICi20842127. VBIAlcBor124741_2233.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM286690 Genomic DNA. Translation: CAL17582.1.
RefSeqiWP_011589412.1. NC_008260.1.

3D structure databases

ProteinModelPortaliQ0VML6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi393595.ABO_2134.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL17582; CAL17582; ABO_2134.
KEGGiabo:ABO_2134.
PATRICi20842127. VBIAlcBor124741_2233.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00031; UER00008.

Family and domain databases

HAMAPiMF_01021. HisI. 1 hit.
InterProiIPR026660. PRA-CH.
IPR002496. PRib_AMP_CycHydrolase_dom.
[Graphical view]
PfamiPF01502. PRA-CH. 1 hit.
[Graphical view]
ProDomiPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Entry informationi

Entry nameiHIS3_ALCBS
AccessioniPrimary (citable) accession number: Q0VML6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: September 5, 2006
Last modified: November 2, 2016
This is version 71 of the entry and version 1 of the sequence. [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

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.