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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: L-histidine biosynthesis

    This protein is involved in step 4 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
    Proteins known to be involved in the 9 steps of the subpathway in this organism are:
    1. ATP phosphoribosyltransferase (hisG)
    2. Phosphoribosyl-ATP pyrophosphatase (hisE)
    3. Phosphoribosyl-AMP cyclohydrolase (hisI)
    4. Phosphoribosyl isomerase A (priA)
    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. Histidinol-phosphatase (hisN)
    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.

    Pathwayi: L-tryptophan biosynthesis

    This protein is involved in step 3 of the subpathway that synthesizes L-tryptophan from chorismate.
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Anthranilate synthase component 1 (trpE)
    2. Anthranilate phosphoribosyltransferase 2 (trpD2), Anthranilate phosphoribosyltransferase 1 (trpD1)
    3. Phosphoribosyl isomerase A (priA)
    4. Indole-3-glycerol phosphate synthase 1 (trpC1), Indole-3-glycerol phosphate synthase 2 (trpC2)
    5. Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA)
    This subpathway is part of the pathway L-tryptophan 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-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei11Proton acceptorBy similarity1
    Active sitei130Proton donorBy similarity1

    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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    Proteomesi
    • UP000001973 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi11D → A: No activity. 1 Publication1
    Mutagenesisi19R → A: No effect on activity toward PRA. No activity toward ProFAR. 1 Publication1
    Mutagenesisi81S → T: No activity toward PRA. Almost no effect on activity toward ProFAR. 1 Publication1
    Mutagenesisi130D → A: Very low activity toward PRA. No activity toward ProFAR. 1 Publication1
    Mutagenesisi130D → Q: No activity. 1 Publication1
    Mutagenesisi166T → A: No activity. 1 Publication1
    Mutagenesisi171D → A: Low activity toward PRA. No activity toward ProFAR. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001420871 – 240Phosphoribosyl isomerase AAdd BLAST240

    Proteomic databases

    PRIDEiP16250.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi100226.SCO2050.

    Structurei

    Secondary structure

    1240
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 13Combined sources9
    Beta strandi16 – 18Combined sources3
    Beta strandi28 – 30Combined sources3
    Helixi34 – 43Combined sources10
    Beta strandi47 – 53Combined sources7
    Helixi54 – 58Combined sources5
    Helixi64 – 73Combined sources10
    Beta strandi75 – 83Combined sources9
    Helixi87 – 95Combined sources9
    Beta strandi99 – 103Combined sources5
    Helixi105 – 109Combined sources5
    Helixi111 – 121Combined sources11
    Helixi122 – 124Combined sources3
    Beta strandi125 – 132Combined sources8
    Beta strandi135 – 138Combined sources4
    Beta strandi139 – 141Combined sources3
    Beta strandi143 – 147Combined sources5
    Helixi148 – 157Combined sources10
    Beta strandi163 – 167Combined sources5
    Helixi168 – 170Combined sources3
    Turni171 – 173Combined sources3
    Helixi179 – 187Combined sources9
    Beta strandi193 – 197Combined sources5
    Helixi202 – 209Combined sources8
    Turni210 – 215Combined sources6
    Beta strandi216 – 221Combined sources6
    Helixi223 – 226Combined sources4
    Helixi232 – 239Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1VZWX-ray1.80A1-240[»]
    2VEPX-ray1.80A1-240[»]
    2X30X-ray1.95A1-240[»]
    5DN1X-ray1.95A1-240[»]
    ProteinModelPortaliP16250.
    SMRiP16250.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16250.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HisA/HisF family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CJV. Bacteria.
    COG0106. LUCA.
    HOGENOMiHOG000224614.
    InParanoidiP16250.
    KOiK01814.
    K01817.
    OMAiEWLHLVD.
    OrthoDBiPOG091H048O.
    PhylomeDBiP16250.

    Family and domain databases

    CDDicd04732. HisA. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01014. HisA. 1 hit.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1VZWX-ray1.80A1-240[»]
    2VEPX-ray1.80A1-240[»]
    2X30X-ray1.95A1-240[»]
    5DN1X-ray1.95A1-240[»]
    ProteinModelPortaliP16250.
    SMRiP16250.
    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

    eggNOGiENOG4105CJV. Bacteria.
    COG0106. LUCA.
    HOGENOMiHOG000224614.
    InParanoidiP16250.
    KOiK01814.
    K01817.
    OMAiEWLHLVD.
    OrthoDBiPOG091H048O.
    PhylomeDBiP16250.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiP16250.

    Family and domain databases

    CDDicd04732. HisA. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01014. HisA. 1 hit.
    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...

    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: November 2, 2016
    This is version 130 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

    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.