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Protein

Phosphoribosyl-AMP cyclohydrolase

Gene

hisI

Organism
Bacillus cereus (strain ZK / E33L)
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 2 (hisC2), Histidinol-phosphate aminotransferase 1 (hisC1)
  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 bindingi71 – 711MagnesiumUniRule annotation
Metal bindingi72 – 721Zinc; shared with dimeric partnerUniRule annotation
Metal bindingi73 – 731MagnesiumUniRule annotation
Metal bindingi75 – 751MagnesiumUniRule annotation
Metal bindingi88 – 881Zinc; shared with dimeric partnerUniRule annotation
Metal bindingi95 – 951Zinc; 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

BioCyciBCER288681:GHG7-1377-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:BCE33L1296
OrganismiBacillus cereus (strain ZK / E33L)
Taxonomic identifieri288681 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000002612 Componenti: Chromosome

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 – 101101Phosphoribosyl-AMP cyclohydrolasePRO_0000229809Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ63DW7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-CH family.UniRule annotation

Phylogenomic databases

KOiK01496.
OMAiICDTLMF.

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.

Q63DW7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPNFSKGLL PAVVIEEGTK EVLMLAYMNE EAYEKTLKTK RTWFYSRSRR
60 70 80 90 100
SLWNKGETSG HVQHVQSLYL DCDQDAIVVV VKQVGPACHT GEKTCFHYKI

I
Length:101
Mass (Da):11,607
Last modified:October 25, 2004 - v1
Checksum:iFDA6E19DE50A01F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000001 Genomic DNA. Translation: AAU18951.1.
RefSeqiWP_000803979.1. NZ_CP009968.1.

Genome annotation databases

EnsemblBacteriaiAAU18951; AAU18951; BCE33L1296.
KEGGibcz:BCE33L1296.
PATRICi18886056. VBIBacCer95304_1367.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000001 Genomic DNA. Translation: AAU18951.1.
RefSeqiWP_000803979.1. NZ_CP009968.1.

3D structure databases

ProteinModelPortaliQ63DW7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAU18951; AAU18951; BCE33L1296.
KEGGibcz:BCE33L1296.
PATRICi18886056. VBIBacCer95304_1367.

Phylogenomic databases

KOiK01496.
OMAiICDTLMF.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00008.
BioCyciBCER288681:GHG7-1377-MONOMER.

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_BACCZ
AccessioniPrimary (citable) accession number: Q63DW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 25, 2004
Last modified: September 7, 2016
This is version 74 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.