TRPD_THEKO
ID TRPD_THEKO Reviewed; 325 AA.
AC Q9YGB4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=TK0253;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=10628865; DOI=10.1007/s004380051145;
RA Tang X., Ezaki S., Fujiwara S., Takagi M., Atomi H., Imanaka T.;
RT "The tryptophan biosynthesis gene cluster trpCDEGFBA from Pyrococcus
RT kodakaraensis KOD1 is regulated at the transcriptional level and expressed
RT as a single mRNA.";
RL Mol. Gen. Genet. 262:815-821(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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 -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_00211}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB030011; BAA82546.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD84442.1; -; Genomic_DNA.
DR PIR; T43923; T43923.
DR RefSeq; WP_011249208.1; NC_006624.1.
DR PDB; 5NOE; X-ray; 1.91 A; A/B/C/D=1-325.
DR PDB; 5NOF; X-ray; 2.42 A; A/B=1-325.
DR PDBsum; 5NOE; -.
DR PDBsum; 5NOF; -.
DR AlphaFoldDB; Q9YGB4; -.
DR SMR; Q9YGB4; -.
DR STRING; 69014.TK0253; -.
DR EnsemblBacteria; BAD84442; BAD84442; TK0253.
DR GeneID; 3234098; -.
DR KEGG; tko:TK0253; -.
DR PATRIC; fig|69014.16.peg.252; -.
DR eggNOG; arCOG02012; Archaea.
DR HOGENOM; CLU_034315_2_1_2; -.
DR InParanoid; Q9YGB4; -.
DR OMA; GPMTNPA; -.
DR OrthoDB; 77838at2157; -.
DR PhylomeDB; Q9YGB4; -.
DR BRENDA; 2.4.2.18; 5246.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000000536; 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..325
FT /note="Anthranilate phosphoribosyltransferase"
FT /id="PRO_0000154521"
FT BINDING 74
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 74
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 77..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 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 84..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 BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 101..109
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 104
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 113
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 159
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT HELIX 2..8
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:5NOE"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:5NOE"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:5NOE"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:5NOE"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5NOE"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:5NOE"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:5NOE"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:5NOE"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:5NOE"
FT STRAND 225..239
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 274..290
FT /evidence="ECO:0007829|PDB:5NOE"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:5NOF"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:5NOE"
FT HELIX 310..324
FT /evidence="ECO:0007829|PDB:5NOE"
SQ SEQUENCE 325 AA; 34346 MW; 0D06E5CF73BF4042 CRC64;
MSLLAKIVDG KNLSFEEAYE LFNELKGSDG VLIGAYLAAL QTKGYTGEEL AGLARAMRDS
AVKLDLGKVA DTAGTGGDGS STINVSTASA LILSAFTRVA KHGNVSITSK SGSANVLEAL
GLNIRVSPER AREMVESTNF TFIFAPAYHP ALRPIMPVRK ALGIKTVFNV IGPLANPADP
AYQVVGVNSP ELLEPVAEAL EFLGVERALV VHGSGMDEVS PHRETLVLEV GNGVERYTLS
PEDFGIEPVK PLPCSSPEES AARIKAVLGG SGRREDRDFI LVNASAALYA SGVAEDFREG
LEMAREALGQ GMLEKLEEIA CLSKS
