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Protein

Anthranilate phosphoribosyltransferase

Gene

trpD

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).UniRule annotation2 Publications

Catalytic activityi

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation1 Publication

Cofactori

Mg2+Note: Binds 2 magnesium ions per monomer.

Kineticsi

  1. KM=50 µM for magnesium (at 60 degrees Celsius and at pH 7.5)2 Publications
  2. KM=40 nM for anthranilate (at 60 degrees Celsius and at pH 7.5)2 Publications
  3. KM=160 µM for phosphoribosylpyrophosphate (at 60 degrees Celsius and at pH 7.5)2 Publications
  4. KM=20 nM for anthranilate (at 25 degrees Celsius and at pH 7.5)2 Publications
  5. KM=26 nM for anthranilate (at 40 degrees Celsius and at pH 7.5)2 Publications
  6. KM=32 nM for anthranilate (at 50 degrees Celsius and at pH 7.5)2 Publications
  7. KM=35 nM for anthranilate (at 60 degrees Celsius and at pH 7.5)2 Publications
  8. KM=500 nM for anthranilate (at 87 degrees Celsius and at pH 7.52 Publications

    Pathwayi: L-tryptophan biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes L-tryptophan from chorismate.UniRule annotation
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Anthranilate synthase component 1 (trpE), Anthranilate synthase component 2 (trpG)
    2. Anthranilate phosphoribosyltransferase (trpD)
    3. N-(5'-phosphoribosyl)anthranilate isomerase (trpF)
    4. Indole-3-glycerol phosphate synthase (trpC)
    5. Tryptophan synthase beta chain 2 (trpB2), Tryptophan synthase beta chain 1 (trpB1), 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei79 – 791Anthranilate 1; via carbonyl oxygen
    Binding sitei87 – 871PhosphoribosylpyrophosphateUniRule annotation2 Publications
    Metal bindingi91 – 911Magnesium 1
    Binding sitei109 – 1091Anthranilate 1
    Binding sitei118 – 1181Phosphoribosylpyrophosphate; via amide nitrogenUniRule annotation2 Publications
    Binding sitei164 – 1641Anthranilate 2
    Metal bindingi223 – 2231Magnesium 2
    Metal bindingi224 – 2241Magnesium 1
    Metal bindingi224 – 2241Magnesium 2

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

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

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciSSOL273057:GCH2-847-MONOMER.
    BRENDAi2.4.2.18. 6163.
    UniPathwayiUPA00035; UER00041.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Anthranilate phosphoribosyltransferaseUniRule annotation (EC:2.4.2.18UniRule annotation)
    Gene namesi
    Name:trpDUniRule annotation
    Ordered Locus Names:SSO0890
    OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
    Taxonomic identifieri273057 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    Proteomesi
    • UP000001974 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1061K → Q: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency dedreases only 10-fold. 1 Publication
    Mutagenesisi107 – 1071H → A: Limited effect on either affinity for anthranilate and catalytic efficiency. 300-fold decrease of the affinity for anthranilate, whereas catalytic efficiency remains nearly unchanged; when associated with A-178. 1 Publication
    Mutagenesisi154 – 1541H → A: Limited effect on either affinity for anthranilate and catalytic efficiency. 1 Publication
    Mutagenesisi164 – 1641R → A: Strong decrease of the affinity for anthranilate, although only a moderate 7-fold decrease in catalytic efficiency. 1 Publication
    Mutagenesisi178 – 1781P → A: 300-fold decrease of the affinity for anthranilate, whereas catalytic efficiency remains nearly unchanged; when associated with A-107.
    Mutagenesisi223 – 2231D → N: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency is unchanged. 1 Publication
    Mutagenesisi224 – 2241E → Q: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency is unchanged. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 345345Anthranilate phosphoribosyltransferasePRO_0000154523Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation4 Publications

    Protein-protein interaction databases

    STRINGi273057.SSO0890.

    Structurei

    Secondary structure

    1
    345
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 119Combined sources
    Helixi18 – 2912Combined sources
    Helixi35 – 4814Combined sources
    Helixi52 – 6514Combined sources
    Beta strandi75 – 795Combined sources
    Helixi90 – 989Combined sources
    Turni99 – 1013Combined sources
    Beta strandi104 – 1085Combined sources
    Beta strandi112 – 1154Combined sources
    Helixi118 – 1258Combined sources
    Helixi133 – 14311Combined sources
    Beta strandi144 – 1496Combined sources
    Helixi150 – 1534Combined sources
    Helixi155 – 1595Combined sources
    Helixi161 – 1677Combined sources
    Helixi172 – 1754Combined sources
    Helixi177 – 1793Combined sources
    Beta strandi186 – 1916Combined sources
    Helixi195 – 20511Combined sources
    Turni207 – 2093Combined sources
    Beta strandi211 – 2188Combined sources
    Turni219 – 2213Combined sources
    Beta strandi222 – 2243Combined sources
    Beta strandi227 – 23711Combined sources
    Beta strandi240 – 2478Combined sources
    Helixi248 – 2514Combined sources
    Helixi258 – 2603Combined sources
    Helixi266 – 27712Combined sources
    Helixi282 – 29817Combined sources
    Beta strandi301 – 3044Combined sources
    Helixi305 – 31612Combined sources
    Helixi319 – 32911Combined sources
    Helixi333 – 3408Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GXBX-ray2.70A/B/C/D1-345[»]
    1O17X-ray2.05A/B/C/D1-345[»]
    1ZXYX-ray2.56A/B/C/D1-345[»]
    1ZYKX-ray2.40A/B/C/D1-345[»]
    2GVQX-ray2.43A/B/C/D1-345[»]
    3GBRX-ray2.25A/B1-345[»]
    ProteinModelPortaliP50384.
    SMRiP50384. Positions 1-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50384.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni77 – 793Phosphoribosylpyrophosphate binding
    Regioni82 – 832Phosphoribosylpyrophosphate binding
    Regioni89 – 924Phosphoribosylpyrophosphate binding
    Regioni106 – 1149Phosphoribosylpyrophosphate binding

    Sequence similaritiesi

    Belongs to the anthranilate phosphoribosyltransferase family.UniRule annotation

    Phylogenomic databases

    eggNOGiarCOG02012. Archaea.
    COG0547. LUCA.
    HOGENOMiHOG000230451.
    InParanoidiP50384.
    KOiK00766.
    OMAiRTVFNIV.

    Family and domain databases

    Gene3Di3.40.1030.10. 2 hits.
    HAMAPiMF_00211. TrpD.
    InterProiIPR005940. Anthranilate_Pribosyl_Tfrase.
    IPR000312. Glycosyl_Trfase_fam3.
    IPR017459. Glycosyl_Trfase_fam3_N_dom.
    [Graphical view]
    PfamiPF02885. Glycos_trans_3N. 1 hit.
    PF00591. Glycos_transf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47648. SSF47648. 1 hit.
    SSF52418. SSF52418. 1 hit.
    TIGRFAMsiTIGR01245. trpD. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P50384-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNINEILKKL INKSDLEINE AEELAKAIIR GEVPEILVSA ILVALRMKGE
    60 70 80 90 100
    SKNEIVGFAR AMRELAIKID VPNAIDTAGT GGDGLGTVNV STASAILLSL
    110 120 130 140 150
    VNPVAKHGNR AVSGKSGSAD VLEALGYNII VPPERAKELV NKTNFVFLFA
    160 170 180 190 200
    QYYHPAMKNV ANVRKTLGIR TIFNILGPLT NPANAKYQLM GVFSKDHLDL
    210 220 230 240 250
    LSKSAYELDF NKIILVYGEP GIDEVSPIGN TFMKIVSKRG IEEVKLNVTD
    260 270 280 290 300
    FGISPIPIEK LIVNSAEDSA IKIVRAFLGK DEHVAEFIKI NTAVALFALD
    310 320 330 340
    RVGDFREGYE YADHLIEKSL DKLNEIISMN GDVTKLKTIV VKSSG
    Length:345
    Mass (Da):37,574
    Last modified:October 1, 1996 - v1
    Checksum:iD51927F4B7AAFA90
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z50014 Genomic DNA. Translation: CAA90309.1.
    AE006641 Genomic DNA. Translation: AAK41173.1.
    PIRiF90239.
    RefSeqiWP_009992305.1. NC_002754.1.

    Genome annotation databases

    EnsemblBacteriaiAAK41173; AAK41173; SSO0890.
    GeneIDi25404352.
    KEGGisso:SSO0890.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z50014 Genomic DNA. Translation: CAA90309.1.
    AE006641 Genomic DNA. Translation: AAK41173.1.
    PIRiF90239.
    RefSeqiWP_009992305.1. NC_002754.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GXBX-ray2.70A/B/C/D1-345[»]
    1O17X-ray2.05A/B/C/D1-345[»]
    1ZXYX-ray2.56A/B/C/D1-345[»]
    1ZYKX-ray2.40A/B/C/D1-345[»]
    2GVQX-ray2.43A/B/C/D1-345[»]
    3GBRX-ray2.25A/B1-345[»]
    ProteinModelPortaliP50384.
    SMRiP50384. Positions 1-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi273057.SSO0890.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK41173; AAK41173; SSO0890.
    GeneIDi25404352.
    KEGGisso:SSO0890.

    Phylogenomic databases

    eggNOGiarCOG02012. Archaea.
    COG0547. LUCA.
    HOGENOMiHOG000230451.
    InParanoidiP50384.
    KOiK00766.
    OMAiRTVFNIV.

    Enzyme and pathway databases

    UniPathwayiUPA00035; UER00041.
    BioCyciSSOL273057:GCH2-847-MONOMER.
    BRENDAi2.4.2.18. 6163.

    Miscellaneous databases

    EvolutionaryTraceiP50384.

    Family and domain databases

    Gene3Di3.40.1030.10. 2 hits.
    HAMAPiMF_00211. TrpD.
    InterProiIPR005940. Anthranilate_Pribosyl_Tfrase.
    IPR000312. Glycosyl_Trfase_fam3.
    IPR017459. Glycosyl_Trfase_fam3_N_dom.
    [Graphical view]
    PfamiPF02885. Glycos_trans_3N. 1 hit.
    PF00591. Glycos_transf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47648. SSF47648. 1 hit.
    SSF52418. SSF52418. 1 hit.
    TIGRFAMsiTIGR01245. trpD. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The tryptophan operon in Sulfolobus solfataricus."
      Tutino M.L., Cubellis M., Sannia G., Marino G.
      Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DSM 5833 / MT-4.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
    3. "Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus."
      Ivens A., Mayans O., Szadkowski H., Wilmanns M., Kirschner K.
      Eur. J. Biochem. 268:2246-2252(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CRYSTALLIZATION, SUBUNIT.
    4. "Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry."
      Mayans O., Ivens A., Nissen L.J., Kirschner K., Wilmanns M.
      EMBO J. 21:3245-3254(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, SUBUNIT.
    5. "Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus."
      Marino M., Deuss M., Svergun D.I., Konarev P.V., Sterner R., Mayans O.
      J. Biol. Chem. 281:21410-21421(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) IN COMPLEX WITH PHOSPHORIBOSYLPYROPHOSPHATE, ANTHRANILATE AND MAGNESIUM IONS, FUNCTION, MUTAGENESIS OF LYS-106; HIS-107; HIS-154; ARG-164; ASP-223 AND GLU-224, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    6. "Activation of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus by removal of magnesium inhibition and acceleration of product release."
      Schlee S., Deuss M., Bruning M., Ivens A., Schwab T., Hellmann N., Mayans O., Sterner R.
      Biochemistry 48:5199-5209(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH PHOSPHORIBOSYLPYROPHOSPHATE AND MAGNESIUM IONS, SUBUNIT.

    Entry informationi

    Entry nameiTRPD_SULSO
    AccessioniPrimary (citable) accession number: P50384
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: November 11, 2015
    This is version 116 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.