TRPD_METS5
ID TRPD_METS5 Reviewed; 343 AA.
AC A4YHE2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Msed_1689;
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=18083856; DOI=10.1128/aem.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
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}.
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DR EMBL; CP000682; ABP95844.1; -; Genomic_DNA.
DR RefSeq; WP_012021631.1; NC_009440.1.
DR AlphaFoldDB; A4YHE2; -.
DR SMR; A4YHE2; -.
DR STRING; 399549.Msed_1689; -.
DR EnsemblBacteria; ABP95844; ABP95844; Msed_1689.
DR GeneID; 5105335; -.
DR GeneID; 59457194; -.
DR KEGG; mse:Msed_1689; -.
DR eggNOG; arCOG02012; Archaea.
DR HOGENOM; CLU_034315_2_1_2; -.
DR OMA; GPMTNPA; -.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000000242; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Glycosyltransferase; Magnesium; Metal-binding; Reference proteome;
KW Transferase; Tryptophan biosynthesis.
FT CHAIN 1..343
FT /note="Anthranilate phosphoribosyltransferase"
FT /id="PRO_1000071744"
FT BINDING 79
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 79
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 82..83
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 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 89..92
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 91
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 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
SQ SEQUENCE 343 AA; 37229 MW; 1117FEB1438C86C0 CRC64;
MDPKEVLKRL TEGVSLSQEE AKELADLIME GSIPEPLVAG ILVALKMKGE TPDEIIGFVN
SMRQHALKLD LRNTLDTAGT GGDGIGTINV STATALAVSS VFPVAKHGNR AASSRSGSAD
FLESLGYNIQ VPPEKAKDLL SRNNFVFLFA QLYHPSMKNV APVRKVLGVR TIFNLLGPLT
NPAGSERQVM GVYSLPFMRK LAEAALKLGY VKLVLVHGEP GLDEVSPQGK TYITEVTGSK
VEEYTYDFSE IIGQPVPVSR LTTTDPLDSV RRVLMASMGR DEAVEKFIRI NVSVALYTAG
LVSDFKDGFE LSEELVRKLP DRIETLVRDN GDPSKIKAIK GSL
