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Protein

Phosphoribosyl isomerase A

Gene

priA

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the isomerization of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR in the biosynthesis pathway for histidine and the isomerization of the aminoaldose PRA to the aminoketose CdRP in the biosynthsis pathway for tryptophan.

Catalytic activityi

1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide.1 Publication
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.1 Publication

Kineticsi

  1. KM=28 µM for ProFAR1 Publication
  2. KM=4 µM for PRA1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei11 – 111Proton acceptorBy similarity
    Active sitei130 – 1301Proton donorBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Histidine biosynthesis, Tryptophan biosynthesis

    Enzyme and pathway databases

    BRENDAi5.3.1.24. 5998.
    UniPathwayiUPA00031; UER00009.
    UPA00035; UER00042.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoribosyl isomerase A
    Alternative name(s):
    1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (EC:5.3.1.16)
    N-(5'-phosphoribosyl)anthranilate isomerase (EC:5.3.1.24)
    Short name:
    PRAI
    Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
    Gene namesi
    Name:priA
    Synonyms:hisA
    Ordered Locus Names:SCO2050
    ORF Names:SC4G6.19c
    OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    Taxonomic identifieri100226 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    ProteomesiUP000001973 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi11 – 111D → A: No activity. 1 Publication
    Mutagenesisi19 – 191R → A: No effect on activity toward PRA. No activity toward ProFAR. 1 Publication
    Mutagenesisi81 – 811S → T: No activity toward PRA. Almost no effect on activity toward ProFAR. 1 Publication
    Mutagenesisi130 – 1301D → A: Very low activity toward PRA. No activity toward ProFAR. 1 Publication
    Mutagenesisi130 – 1301D → Q: No activity. 1 Publication
    Mutagenesisi166 – 1661T → A: No activity. 1 Publication
    Mutagenesisi171 – 1711D → A: Low activity toward PRA. No activity toward ProFAR. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 240240Phosphoribosyl isomerase APRO_0000142087Add
    BLAST

    Proteomic databases

    PRIDEiP16250.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi100226.SCO2050.

    Structurei

    Secondary structure

    1
    240
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139Combined sources
    Beta strandi16 – 183Combined sources
    Beta strandi28 – 303Combined sources
    Helixi34 – 4310Combined sources
    Beta strandi47 – 537Combined sources
    Helixi54 – 585Combined sources
    Helixi64 – 7310Combined sources
    Beta strandi75 – 839Combined sources
    Helixi87 – 959Combined sources
    Beta strandi99 – 1035Combined sources
    Helixi105 – 1095Combined sources
    Helixi111 – 12111Combined sources
    Helixi122 – 1243Combined sources
    Beta strandi125 – 1328Combined sources
    Beta strandi139 – 1413Combined sources
    Helixi148 – 15710Combined sources
    Beta strandi163 – 1675Combined sources
    Helixi168 – 1703Combined sources
    Turni171 – 1733Combined sources
    Helixi179 – 1879Combined sources
    Beta strandi193 – 1975Combined sources
    Helixi202 – 2098Combined sources
    Turni210 – 2156Combined sources
    Beta strandi216 – 2216Combined sources
    Helixi223 – 2264Combined sources
    Helixi232 – 2398Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VZWX-ray1.80A1-240[»]
    2VEPX-ray1.80A1-240[»]
    2X30X-ray1.95A1-240[»]
    ProteinModelPortaliP16250.
    SMRiP16250. Positions 1-240.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16250.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HisA/HisF family.Curated

    Phylogenomic databases

    eggNOGiCOG0106.
    HOGENOMiHOG000224614.
    InParanoidiP16250.
    KOiK01814.
    K01817.
    OMAiHCVRLKQ.
    OrthoDBiEOG6H1Q3W.
    PhylomeDBiP16250.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01014. HisA.
    InterProiIPR013785. Aldolase_TIM.
    IPR006062. His_biosynth.
    IPR010188. HisA_TrpF.
    IPR023016. Isoase_HisA.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view]
    PfamiPF00977. His_biosynth. 1 hit.
    [Graphical view]
    SUPFAMiSSF51366. SSF51366. 1 hit.
    TIGRFAMsiTIGR01919. hisA-trpF. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P16250-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKLELLPAV DVRDGQAVRL VHGESGTETS YGSPLEAALA WQRSGAEWLH
    60 70 80 90 100
    LVDLDAAFGT GDNRALIAEV AQAMDIKVEL SGGIRDDDTL AAALATGCTR
    110 120 130 140 150
    VNLGTAALET PEWVAKVIAE HGDKIAVGLD VRGTTLRGRG WTRDGGDLYE
    160 170 180 190 200
    TLDRLNKEGC ARYVVTDIAK DGTLQGPNLE LLKNVCAATD RPVVASGGVS
    210 220 230 240
    SLDDLRAIAG LVPAGVEGAI VGKALYAKAF TLEEALEATS
    Length:240
    Mass (Da):25,080
    Last modified:August 1, 1990 - v1
    Checksum:iA150E831DDABC76F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M31628 Genomic DNA. Translation: AAA26760.1.
    AL939111 Genomic DNA. Translation: CAB51442.1.
    PIRiJQ0641.
    RefSeqiNP_626310.1. NC_003888.3.
    WP_003976766.1. NC_003888.3.

    Genome annotation databases

    EnsemblBacteriaiCAB51442; CAB51442; CAB51442.
    GeneIDi1097484.
    KEGGisco:SCO2050.
    PATRICi23733744. VBIStrCoe124346_2081.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M31628 Genomic DNA. Translation: AAA26760.1.
    AL939111 Genomic DNA. Translation: CAB51442.1.
    PIRiJQ0641.
    RefSeqiNP_626310.1. NC_003888.3.
    WP_003976766.1. NC_003888.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VZWX-ray1.80A1-240[»]
    2VEPX-ray1.80A1-240[»]
    2X30X-ray1.95A1-240[»]
    ProteinModelPortaliP16250.
    SMRiP16250. Positions 1-240.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi100226.SCO2050.

    Proteomic databases

    PRIDEiP16250.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB51442; CAB51442; CAB51442.
    GeneIDi1097484.
    KEGGisco:SCO2050.
    PATRICi23733744. VBIStrCoe124346_2081.

    Phylogenomic databases

    eggNOGiCOG0106.
    HOGENOMiHOG000224614.
    InParanoidiP16250.
    KOiK01814.
    K01817.
    OMAiHCVRLKQ.
    OrthoDBiEOG6H1Q3W.
    PhylomeDBiP16250.

    Enzyme and pathway databases

    UniPathwayiUPA00031; UER00009.
    UPA00035; UER00042.
    BRENDAi5.3.1.24. 5998.

    Miscellaneous databases

    EvolutionaryTraceiP16250.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01014. HisA.
    InterProiIPR013785. Aldolase_TIM.
    IPR006062. His_biosynth.
    IPR010188. HisA_TrpF.
    IPR023016. Isoase_HisA.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view]
    PfamiPF00977. His_biosynth. 1 hit.
    [Graphical view]
    SUPFAMiSSF51366. SSF51366. 1 hit.
    TIGRFAMsiTIGR01919. hisA-trpF. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and characterization of the histidine biosynthetic gene cluster of Streptomyces coelicolor A3(2)."
      Limauro D., Avitabile A., Cappellano M., Puglia A.M., Bruni C.B.
      Gene 90:31-41(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: A3(2) / NRRL B-16638.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-471 / A3(2) / M145.
    3. "Occurrence of a putative ancient-like isomerase involved in histidine and tryptophan biosynthesis."
      Barona-Gomez F., Hodgson D.A.
      EMBO Rep. 4:296-300(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HISTIDINE AND TRYPTOPHAN BIOSYNTHESIS.
      Strain: ATCC BAA-471 / A3(2) / M145.
    4. "Two-fold repeated (beta alpha)4 half-barrels may provide a molecular tool for dual substrate specificity."
      Kuper J., Doenges C., Wilmanns M.
      EMBO Rep. 6:134-139(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    5. "The structure/function relationship of a dual-substrate (beta alpha)8-isomerase."
      Wright H., Noda-Garcia L., Ochoa-Leyva A., Hodgson D.A., Fueloep V., Barona-Gomez F.
      Biochem. Biophys. Res. Commun. 365:16-21(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS OF ASP-11; ARG-19; SER-81; ASP-130; THR-166 AND ASP-171.

    Entry informationi

    Entry nameiHIS4_STRCO
    AccessioniPrimary (citable) accession number: P16250
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: May 27, 2015
    This is version 120 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.