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Protein

Phosphoribosyl-AMP cyclohydrolase

Gene

hisI

Organism
Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9)
Status
Reviewed-Annotation score: -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. no protein annotated in this organism
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. no protein annotated in this organism
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 bindingi76MagnesiumUniRule annotation1
Metal bindingi77Zinc; shared with dimeric partnerUniRule annotation1
Metal bindingi78MagnesiumUniRule annotation1
Metal bindingi80MagnesiumUniRule annotation1
Metal bindingi93Zinc; shared with dimeric partnerUniRule annotation1
Metal bindingi100Zinc; 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:STER_1199
OrganismiStreptococcus thermophilus (strain ATCC BAA-491 / LMD-9)
Taxonomic identifieri322159 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000634381 – 112Phosphoribosyl-AMP cyclohydrolaseAdd BLAST112

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ03K83
SMRiQ03K83
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-CH family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000277504
KOiK01496
OMAiTGYRSCF

Family and domain databases

Gene3Di3.10.20.400, 1 hit
HAMAPiMF_01021 HisI, 1 hit
InterProiView protein in InterPro
IPR026660 PRA-CH
IPR002496 PRib_AMP_CycHydrolase_dom
IPR038019 PRib_AMP_CycHydrolase_sf
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
SUPFAMiSSF141734 SSF141734, 1 hit

Sequencei

Sequence statusi: Complete.

Q03K83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEVKLDFDK QGGLVPVIVT DYKTGQVLML AYMNEVSYQL TLETKQMHYW
60 70 80 90 100
SRSRNELWHK GATSGHFQHV KSIKTDCDWD TLLIAVEQEG AACHTGAYSC
110
FFTDIYDDNQ DR
Length:112
Mass (Da):12,916
Last modified:November 14, 2006 - v1
Checksum:i467927928E6C05F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000419 Genomic DNA Translation: ABJ66389.1
RefSeqiWP_011681264.1, NC_008532.1

Genome annotation databases

EnsemblBacteriaiABJ66389; ABJ66389; STER_1199
GeneIDi31937969
KEGGiste:STER_1199

Similar proteinsi

Entry informationi

Entry nameiHIS3_STRTD
AccessioniPrimary (citable) accession number: Q03K83
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 14, 2006
Last modified: February 28, 2018
This is version 69 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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