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Protein

Phosphoribosyl-AMP cyclohydrolase

Gene

hisI

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
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

Pathway: 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)
  2. no protein annotated in this organism
  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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi76 – 761MagnesiumUniRule annotation
Metal bindingi77 – 771Zinc; shared with dimeric partnerUniRule annotation
Metal bindingi78 – 781MagnesiumUniRule annotation
Metal bindingi80 – 801MagnesiumUniRule annotation
Metal bindingi94 – 941Zinc; shared with dimeric partnerUniRule annotation
Metal bindingi101 – 1011Zinc; 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

BioCyciDVUL882:GJIL-121-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:DVU_0113
OrganismiDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Taxonomic identifieri882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
ProteomesiUP000002194 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 – 126126Phosphoribosyl-AMP cyclohydrolasePRO_0000136476Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi882.DVU0113.

Structurei

3D structure databases

ProteinModelPortaliP62386.
SMRiP62386. Positions 3-121.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-CH family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0139.
KOiK01496.
OMAiGACHVGY.
OrthoDBiEOG6PGKB6.
PhylomeDBiP62386.

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.

P62386-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAFVPDFGK AGGLVPAIAQ DADTGEVLMM AWMNAEAFEM TLKTGEAHYF
60 70 80 90 100
SRSRGRLWHK GGTSGHTQHI RAVRLDCDSD TILLLVEQRG GAACHEGYRS
110 120
CFYREMKDGE VSICSPKVFD PKEVYK
Length:126
Mass (Da):13,991
Last modified:July 5, 2004 - v1
Checksum:iAD4F63840DC10E29
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017285 Genomic DNA. Translation: AAS94597.1.
RefSeqiWP_010937424.1. NC_002937.3.
YP_009338.1. NC_002937.3.

Genome annotation databases

EnsemblBacteriaiAAS94597; AAS94597; DVU_0113.
GeneIDi2794982.
KEGGidvu:DVU0113.
PATRICi32060210. VBIDesVul119526_0111.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017285 Genomic DNA. Translation: AAS94597.1.
RefSeqiWP_010937424.1. NC_002937.3.
YP_009338.1. NC_002937.3.

3D structure databases

ProteinModelPortaliP62386.
SMRiP62386. Positions 3-121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi882.DVU0113.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS94597; AAS94597; DVU_0113.
GeneIDi2794982.
KEGGidvu:DVU0113.
PATRICi32060210. VBIDesVul119526_0111.

Phylogenomic databases

eggNOGiCOG0139.
KOiK01496.
OMAiGACHVGY.
OrthoDBiEOG6PGKB6.
PhylomeDBiP62386.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00008.
BioCyciDVUL882:GJIL-121-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hildenborough / ATCC 29579 / NCIMB 8303.

Entry informationi

Entry nameiHIS3_DESVH
AccessioniPrimary (citable) accession number: P62386
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: May 27, 2015
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

External Data

Dasty 3

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 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.