TRPD_THET8
ID TRPD_THET8 Reviewed; 329 AA.
AC Q5SH88;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=TTHA1842;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), AND SUBUNIT.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of TTHA1842 from Thermus thermophilus HB8.";
RL Submitted (JUL-2011) to the PDB data bank.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00211};
CC Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP-
CC Rule:MF_00211};
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|Ref.2}.
CC -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_00211}.
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DR EMBL; AP008226; BAD71665.1; -; Genomic_DNA.
DR RefSeq; WP_011173866.1; NC_006461.1.
DR RefSeq; YP_145108.1; NC_006461.1.
DR PDB; 2ELC; X-ray; 1.55 A; A/B/C/D=1-329.
DR PDBsum; 2ELC; -.
DR AlphaFoldDB; Q5SH88; -.
DR SMR; Q5SH88; -.
DR STRING; 300852.55773224; -.
DR EnsemblBacteria; BAD71665; BAD71665; BAD71665.
DR GeneID; 3169363; -.
DR KEGG; ttj:TTHA1842; -.
DR PATRIC; fig|300852.9.peg.1813; -.
DR eggNOG; COG0547; Bacteria.
DR HOGENOM; CLU_034315_2_1_0; -.
DR OMA; GPMTNPA; -.
DR PhylomeDB; Q5SH88; -.
DR UniPathway; UPA00035; UER00041.
DR EvolutionaryTrace; Q5SH88; -.
DR Proteomes; UP000000532; Chromosome.
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; IEA:UniProtKB-UniRule.
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..329
FT /note="Anthranilate phosphoribosyltransferase"
FT /id="PRO_0000227196"
FT BINDING 78
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 78
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 81..82
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 88..91
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 106..114
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 109
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
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 BINDING 164
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:2ELC"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:2ELC"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:2ELC"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:2ELC"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:2ELC"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2ELC"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:2ELC"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:2ELC"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2ELC"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2ELC"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:2ELC"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 278..293
FT /evidence="ECO:0007829|PDB:2ELC"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 300..313
FT /evidence="ECO:0007829|PDB:2ELC"
FT HELIX 315..328
FT /evidence="ECO:0007829|PDB:2ELC"
SQ SEQUENCE 329 AA; 34275 MW; C18C6A8C40C513A6 CRC64;
MDAVKKAILG EVLEEEEAYE VMRALMAGEV SPVRAAGLLV ALSLRGERPH EIAAMARAMR
EAARPLRVHR RPLLDIVGTG GDGKGLMNLS TLAALVAAAG GVAVAKHGNR AASSRAGSAD
LLEALGVDLE APPERVGEAI EELGFGFLFA RVFHPAMRHV APVRAELGVR TVFNLLGPLT
NPAGADAYVL GVFSPEWLAP MAEALERLGA RGLVVHGEGA DELVLGENRV VEVGKGAYAL
TPEEVGLKRA PLEALKGGGP EENAALARRL LKGEEKGPLA DAVALAAGAG FYAAGKTPSL
KEGVALAREV LASGEAYLLL ERYVAFLRA
