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Protein

Phosphoribosyl-AMP cyclohydrolase

Gene

hisI

Organism
Burkholderia pseudomallei (strain 1106a)
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)
  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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi83 – 831MagnesiumUniRule annotation
Metal bindingi84 – 841Zinc; shared with dimeric partnerUniRule annotation
Metal bindingi85 – 851MagnesiumUniRule annotation
Metal bindingi87 – 871MagnesiumUniRule annotation
Metal bindingi101 – 1011Zinc; shared with dimeric partnerUniRule annotation
Metal bindingi108 – 1081Zinc; shared with dimeric partnerUniRule annotation

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

BioCyciBPSE357348:GHVF-3718-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:BURPS1106A_3717
OrganismiBurkholderia pseudomallei (strain 1106a)
Taxonomic identifieri357348 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000006738 Componenti: Chromosome I

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 137137Phosphoribosyl-AMP cyclohydrolasePRO_1000063397Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA3P026.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-CH family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000277504.
KOiK01496.
OMAiGPACHTN.
OrthoDBiEOG6PGKB6.

Family and domain databases

HAMAPiMF_01021. HisI.
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.

A3P026-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAEAKPGDW LGKVRWDANG LVPVIAQDAA TNDVLMFAWM NRDALAKTIE
60 70 80 90 100
LKRAVYYSRS RQRLWFKGEE SGHVQHVHEV RLDCDEDVVL LKVEQVEGIA
110 120 130
CHTGRRSCFF QKFEGTVDDG EWVAVDPVLK DPEHIYK
Length:137
Mass (Da):15,699
Last modified:April 3, 2007 - v1
Checksum:iD792C45902D6F457
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000572 Genomic DNA. Translation: ABN91984.1.
RefSeqiWP_004201279.1. NC_009076.1.

Genome annotation databases

EnsemblBacteriaiABN91984; ABN91984; BURPS1106A_3717.
KEGGibpl:BURPS1106A_3717.
PATRICi19225737. VBIBurPse14980_3505.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000572 Genomic DNA. Translation: ABN91984.1.
RefSeqiWP_004201279.1. NC_009076.1.

3D structure databases

ProteinModelPortaliA3P026.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN91984; ABN91984; BURPS1106A_3717.
KEGGibpl:BURPS1106A_3717.
PATRICi19225737. VBIBurPse14980_3505.

Phylogenomic databases

HOGENOMiHOG000277504.
KOiK01496.
OMAiGPACHTN.
OrthoDBiEOG6PGKB6.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00008.
BioCyciBPSE357348:GHVF-3718-MONOMER.

Family and domain databases

HAMAPiMF_01021. HisI.
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...

Publicationsi

  1. DeShazer D., Woods D.E., Nierman W.C.
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1106a.

Entry informationi

Entry nameiHIS3_BURP0
AccessioniPrimary (citable) accession number: A3P026
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 3, 2007
Last modified: November 11, 2015
This is version 56 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

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.