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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)DescriptionActionsGraphical viewLength
    Binding sitei79Anthranilate 1; via carbonyl oxygen1
    Binding sitei87PhosphoribosylpyrophosphateUniRule annotation2 Publications1
    Metal bindingi91Magnesium 11
    Binding sitei109Anthranilate 11
    Binding sitei118Phosphoribosylpyrophosphate; via amide nitrogenUniRule annotation2 Publications1
    Binding sitei164Anthranilate 21
    Metal bindingi223Magnesium 21
    Metal bindingi224Magnesium 11
    Metal bindingi224Magnesium 21

    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

    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

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi106K → Q: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency dedreases only 10-fold. 1 Publication1
    Mutagenesisi107H → 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 Publication1
    Mutagenesisi154H → A: Limited effect on either affinity for anthranilate and catalytic efficiency. 1 Publication1
    Mutagenesisi164R → A: Strong decrease of the affinity for anthranilate, although only a moderate 7-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi178P → A: 300-fold decrease of the affinity for anthranilate, whereas catalytic efficiency remains nearly unchanged; when associated with A-107. 1
    Mutagenesisi223D → N: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency is unchanged. 1 Publication1
    Mutagenesisi224E → Q: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency is unchanged. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001545231 – 345Anthranilate phosphoribosyltransferaseAdd BLAST345

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation4 Publications

    Protein-protein interaction databases

    STRINGi273057.SSO0890.

    Structurei

    Secondary structure

    1345
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 11Combined sources9
    Helixi18 – 29Combined sources12
    Helixi35 – 48Combined sources14
    Helixi52 – 65Combined sources14
    Beta strandi75 – 79Combined sources5
    Helixi90 – 98Combined sources9
    Turni99 – 101Combined sources3
    Beta strandi104 – 108Combined sources5
    Beta strandi112 – 115Combined sources4
    Helixi118 – 125Combined sources8
    Helixi133 – 143Combined sources11
    Beta strandi144 – 149Combined sources6
    Helixi150 – 153Combined sources4
    Helixi155 – 159Combined sources5
    Helixi161 – 167Combined sources7
    Helixi172 – 175Combined sources4
    Helixi177 – 179Combined sources3
    Beta strandi186 – 191Combined sources6
    Helixi195 – 205Combined sources11
    Turni207 – 209Combined sources3
    Beta strandi211 – 218Combined sources8
    Turni219 – 221Combined sources3
    Beta strandi222 – 224Combined sources3
    Beta strandi227 – 237Combined sources11
    Beta strandi240 – 247Combined sources8
    Helixi248 – 251Combined sources4
    Helixi258 – 260Combined sources3
    Helixi266 – 277Combined sources12
    Helixi282 – 298Combined sources17
    Beta strandi301 – 304Combined sources4
    Helixi305 – 316Combined sources12
    Helixi319 – 329Combined sources11
    Helixi333 – 340Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50384.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni77 – 79Phosphoribosylpyrophosphate binding3
    Regioni82 – 83Phosphoribosylpyrophosphate binding2
    Regioni89 – 92Phosphoribosylpyrophosphate binding4
    Regioni106 – 114Phosphoribosylpyrophosphate binding9

    Sequence similaritiesi

    Belongs to the anthranilate phosphoribosyltransferase family.UniRule annotation

    Phylogenomic databases

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

    Family and domain databases

    Gene3Di3.40.1030.10. 2 hits.
    HAMAPiMF_00211. TrpD. 1 hit.
    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.
    GeneIDi27427211.
    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi273057.SSO0890.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK41173; AAK41173; SSO0890.
    GeneIDi27427211.
    KEGGisso:SSO0890.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayiUPA00035; UER00041.
    BRENDAi2.4.2.18. 6163.

    Miscellaneous databases

    EvolutionaryTraceiP50384.

    Family and domain databases

    Gene3Di3.40.1030.10. 2 hits.
    HAMAPiMF_00211. TrpD. 1 hit.
    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...

    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 30, 2016
    This is version 122 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.