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P16250

- HIS4_STRCO

UniProt

P16250 - HIS4_STRCO

Protein

Phosphoribosyl isomerase A

Gene

priA

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    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

    1. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity Source: UniProtKB-HAMAP
    2. phosphoribosylanthranilate isomerase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. histidine biosynthetic process Source: UniProtKB-HAMAP
    2. tryptophan biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    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: Chromosome

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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 – 139
    Beta strandi16 – 183
    Beta strandi28 – 303
    Helixi34 – 4310
    Beta strandi47 – 537
    Helixi54 – 585
    Helixi64 – 7310
    Beta strandi75 – 839
    Helixi87 – 959
    Beta strandi99 – 1035
    Helixi105 – 1095
    Helixi111 – 12111
    Helixi122 – 1243
    Beta strandi125 – 1328
    Beta strandi139 – 1413
    Helixi148 – 15710
    Beta strandi163 – 1675
    Helixi168 – 1703
    Turni171 – 1733
    Helixi179 – 1879
    Beta strandi193 – 1975
    Helixi202 – 2098
    Turni210 – 2156
    Beta strandi216 – 2216
    Helixi223 – 2264
    Helixi232 – 2398

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK01814.
    K01817.
    OMAiQRDYGSD.
    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

    MSKLELLPAV DVRDGQAVRL VHGESGTETS YGSPLEAALA WQRSGAEWLH    50
    LVDLDAAFGT GDNRALIAEV AQAMDIKVEL SGGIRDDDTL AAALATGCTR 100
    VNLGTAALET PEWVAKVIAE HGDKIAVGLD VRGTTLRGRG WTRDGGDLYE 150
    TLDRLNKEGC ARYVVTDIAK DGTLQGPNLE LLKNVCAATD RPVVASGGVS 200
    SLDDLRAIAG LVPAGVEGAI VGKALYAKAF TLEEALEATS 240
    Length:240
    Mass (Da):25,080
    Last modified:August 1, 1990 - v1
    Checksum:iA150E831DDABC76F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31628 Genomic DNA. Translation: AAA26760.1.
    AL939111 Genomic DNA. Translation: CAB51442.1.
    PIRiJQ0641.
    RefSeqiNP_626310.1. NC_003888.3.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31628 Genomic DNA. Translation: AAA26760.1 .
    AL939111 Genomic DNA. Translation: CAB51442.1 .
    PIRi JQ0641.
    RefSeqi NP_626310.1. NC_003888.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VZW X-ray 1.80 A 1-240 [» ]
    2VEP X-ray 1.80 A 1-240 [» ]
    2X30 X-ray 1.95 A 1-240 [» ]
    ProteinModelPortali P16250.
    SMRi P16250. Positions 1-240.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 100226.SCO2050.

    Proteomic databases

    PRIDEi P16250.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB51442 ; CAB51442 ; CAB51442 .
    GeneIDi 1097484.
    KEGGi sco:SCO2050.
    PATRICi 23733744. VBIStrCoe124346_2081.

    Phylogenomic databases

    eggNOGi COG0106.
    HOGENOMi HOG000224614.
    KOi K01814.
    K01817.
    OMAi QRDYGSD.
    OrthoDBi EOG6H1Q3W.
    PhylomeDBi P16250.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00009 .
    UPA00035 ; UER00042 .

    Miscellaneous databases

    EvolutionaryTracei P16250.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01014. HisA.
    InterProi IPR013785. Aldolase_TIM.
    IPR006062. His_biosynth.
    IPR010188. HisA_TrpF.
    IPR023016. Isoase_HisA.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view ]
    Pfami PF00977. His_biosynth. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51366. SSF51366. 1 hit.
    TIGRFAMsi TIGR01919. hisA-trpF. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 115 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