TRPD_SACS2
ID TRPD_SACS2 Reviewed; 345 AA.
AC P50384;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00211};
DE EC=2.4.2.18 {ECO:0000255|HAMAP-Rule:MF_00211};
GN Name=trpD {ECO:0000255|HAMAP-Rule:MF_00211}; OrderedLocusNames=SSO0890;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 5833 / MT-4;
RA Tutino M.L., Cubellis M., Sannia G., Marino G.;
RT "The tryptophan operon in Sulfolobus solfataricus.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=11298741; DOI=10.1046/j.1432-1327.2001.02102.x;
RA Ivens A., Mayans O., Szadkowski H., Wilmanns M., Kirschner K.;
RT "Purification, characterization and crystallization of thermostable
RT anthranilate phosphoribosyltransferase from Sulfolobus solfataricus.";
RL Eur. J. Biochem. 268:2246-2252(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, AND
RP SUBUNIT.
RX PubMed=12093726; DOI=10.1093/emboj/cdf298;
RA Mayans O., Ivens A., Nissen L.J., Kirschner K., Wilmanns M.;
RT "Structural analysis of two enzymes catalysing reverse metabolic reactions
RT implies common ancestry.";
RL EMBO J. 21:3245-3254(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) IN COMPLEX WITH
RP PHOSPHORIBOSYLPYROPHOSPHATE, ANTHRANILATE AND MAGNESIUM IONS, FUNCTION,
RP MUTAGENESIS OF LYS-106; HIS-107; HIS-154; ARG-164; ASP-223 AND GLU-224,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=16714288; DOI=10.1074/jbc.m601403200;
RA Marino M., Deuss M., Svergun D.I., Konarev P.V., Sterner R., Mayans O.;
RT "Structural and mutational analysis of substrate complexation by
RT anthranilate phosphoribosyltransferase from Sulfolobus solfataricus.";
RL J. Biol. Chem. 281:21410-21421(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH
RP PHOSPHORIBOSYLPYROPHOSPHATE AND MAGNESIUM IONS, AND SUBUNIT.
RX PubMed=19385665; DOI=10.1021/bi802335s;
RA Schlee S., Deuss M., Bruning M., Ivens A., Schwab T., Hellmann N.,
RA Mayans O., Sterner R.;
RT "Activation of anthranilate phosphoribosyltransferase from Sulfolobus
RT solfataricus by removal of magnesium inhibition and acceleration of product
RT release.";
RL Biochemistry 48:5199-5209(2009).
CC -!- FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5-
CC phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-
CC phosphoribosyl)-anthranilate (PRA). {ECO:0000255|HAMAP-Rule:MF_00211,
CC ECO:0000269|PubMed:11298741, ECO:0000269|PubMed:16714288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + anthranilate;
CC Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00211,
CC ECO:0000269|PubMed:11298741};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 2 magnesium ions per monomer.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for magnesium (at 60 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:11298741, ECO:0000269|PubMed:16714288};
CC KM=40 nM for anthranilate (at 60 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:11298741, ECO:0000269|PubMed:16714288};
CC KM=160 uM for phosphoribosylpyrophosphate (at 60 degrees Celsius and
CC at pH 7.5) {ECO:0000269|PubMed:11298741,
CC ECO:0000269|PubMed:16714288};
CC KM=20 nM for anthranilate (at 25 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:11298741, ECO:0000269|PubMed:16714288};
CC KM=26 nM for anthranilate (at 40 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:11298741, ECO:0000269|PubMed:16714288};
CC KM=32 nM for anthranilate (at 50 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:11298741, ECO:0000269|PubMed:16714288};
CC KM=35 nM for anthranilate (at 60 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:11298741, ECO:0000269|PubMed:16714288};
CC KM=500 nM for anthranilate (at 87 degrees Celsius and at pH 7.5
CC {ECO:0000269|PubMed:11298741, ECO:0000269|PubMed:16714288};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 2/5. {ECO:0000255|HAMAP-
CC Rule:MF_00211}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00211,
CC ECO:0000269|PubMed:11298741, ECO:0000269|PubMed:12093726,
CC ECO:0000269|PubMed:16714288, ECO:0000269|PubMed:19385665}.
CC -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_00211}.
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DR EMBL; Z50014; CAA90309.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41173.1; -; Genomic_DNA.
DR PIR; F90239; F90239.
DR RefSeq; WP_009992305.1; NC_002754.1.
DR PDB; 1GXB; X-ray; 2.70 A; A/B/C/D=1-345.
DR PDB; 1O17; X-ray; 2.05 A; A/B/C/D=1-345.
DR PDB; 1ZXY; X-ray; 2.56 A; A/B/C/D=1-345.
DR PDB; 1ZYK; X-ray; 2.40 A; A/B/C/D=1-345.
DR PDB; 2GVQ; X-ray; 2.43 A; A/B/C/D=1-345.
DR PDB; 3GBR; X-ray; 2.25 A; A/B=1-345.
DR PDBsum; 1GXB; -.
DR PDBsum; 1O17; -.
DR PDBsum; 1ZXY; -.
DR PDBsum; 1ZYK; -.
DR PDBsum; 2GVQ; -.
DR PDBsum; 3GBR; -.
DR AlphaFoldDB; P50384; -.
DR SMR; P50384; -.
DR STRING; 273057.SSO0890; -.
DR EnsemblBacteria; AAK41173; AAK41173; SSO0890.
DR GeneID; 44129821; -.
DR KEGG; sso:SSO0890; -.
DR PATRIC; fig|273057.12.peg.894; -.
DR eggNOG; arCOG02012; Archaea.
DR HOGENOM; CLU_034315_2_1_2; -.
DR InParanoid; P50384; -.
DR OMA; GPMTNPA; -.
DR PhylomeDB; P50384; -.
DR BRENDA; 2.4.2.18; 6163.
DR SABIO-RK; P50384; -.
DR UniPathway; UPA00035; UER00041.
DR EvolutionaryTrace; P50384; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.1030.10; -; 1.
DR HAMAP; MF_00211; TrpD; 1.
DR InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR InterPro; IPR035902; Nuc_phospho_transferase.
DR PANTHER; PTHR43285; PTHR43285; 1.
DR Pfam; PF02885; Glycos_trans_3N; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR SUPFAM; SSF47648; SSF47648; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR TIGRFAMs; TIGR01245; trpD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Glycosyltransferase; Magnesium; Metal-binding; Reference proteome;
KW Transferase; Tryptophan biosynthesis.
FT CHAIN 1..345
FT /note="Anthranilate phosphoribosyltransferase"
FT /id="PRO_0000154523"
FT BINDING 77..79
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT BINDING 79
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT BINDING 82..83
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT BINDING 87
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211,
FT ECO:0000269|PubMed:16714288, ECO:0000269|PubMed:19385665"
FT BINDING 89..92
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 106..114
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT BINDING 109
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT BINDING 118
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211,
FT ECO:0000269|PubMed:16714288, ECO:0000269|PubMed:19385665"
FT BINDING 164
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT MUTAGEN 106
FT /note="K->Q: Affinity for phosphoribosylpyrophosphate is
FT similar to that of the wild-type enzyme and catalytic
FT efficiency dedreases only 10-fold."
FT /evidence="ECO:0000269|PubMed:16714288"
FT MUTAGEN 107
FT /note="H->A: Limited effect on either affinity for
FT anthranilate and catalytic efficiency. 300-fold decrease of
FT the affinity for anthranilate, whereas catalytic efficiency
FT remains nearly unchanged; when associated with A-178."
FT /evidence="ECO:0000269|PubMed:16714288"
FT MUTAGEN 154
FT /note="H->A: Limited effect on either affinity for
FT anthranilate and catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:16714288"
FT MUTAGEN 164
FT /note="R->A: Strong decrease of the affinity for
FT anthranilate, although only a moderate 7-fold decrease in
FT catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:16714288"
FT MUTAGEN 178
FT /note="P->A: 300-fold decrease of the affinity for
FT anthranilate, whereas catalytic efficiency remains nearly
FT unchanged; when associated with A-107."
FT MUTAGEN 223
FT /note="D->N: Affinity for phosphoribosylpyrophosphate is
FT similar to that of the wild-type enzyme and catalytic
FT efficiency is unchanged."
FT /evidence="ECO:0000269|PubMed:16714288"
FT MUTAGEN 224
FT /note="E->Q: Affinity for phosphoribosylpyrophosphate is
FT similar to that of the wild-type enzyme and catalytic
FT efficiency is unchanged."
FT /evidence="ECO:0000269|PubMed:16714288"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:1O17"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3GBR"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:1O17"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1O17"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1O17"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:1O17"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1O17"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:1O17"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1ZYK"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:1O17"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:1O17"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1O17"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:1O17"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 266..277
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 282..298
FT /evidence="ECO:0007829|PDB:1O17"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 305..316
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:1O17"
FT HELIX 333..340
FT /evidence="ECO:0007829|PDB:1O17"
SQ SEQUENCE 345 AA; 37574 MW; D51927F4B7AAFA90 CRC64;
MNINEILKKL INKSDLEINE AEELAKAIIR GEVPEILVSA ILVALRMKGE SKNEIVGFAR
AMRELAIKID VPNAIDTAGT GGDGLGTVNV STASAILLSL VNPVAKHGNR AVSGKSGSAD
VLEALGYNII VPPERAKELV NKTNFVFLFA QYYHPAMKNV ANVRKTLGIR TIFNILGPLT
NPANAKYQLM GVFSKDHLDL LSKSAYELDF NKIILVYGEP GIDEVSPIGN TFMKIVSKRG
IEEVKLNVTD FGISPIPIEK LIVNSAEDSA IKIVRAFLGK DEHVAEFIKI NTAVALFALD
RVGDFREGYE YADHLIEKSL DKLNEIISMN GDVTKLKTIV VKSSG
