ID A0A4Q0IGA0_9BACT Unreviewed; 332 AA. AC A0A4Q0IGA0; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 24-JAN-2024, entry version 15. DE RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00211}; DE EC=2.4.2.18 {ECO:0000256|HAMAP-Rule:MF_00211}; GN Name=trpD {ECO:0000256|HAMAP-Rule:MF_00211, GN ECO:0000313|EMBL:RXE63760.1}; GN ORFNames=ED388_14235 {ECO:0000313|EMBL:RXE63760.1}; OS Muribaculaceae bacterium Isolate-007 (NCI). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae. OX NCBI_TaxID=2489217 {ECO:0000313|EMBL:RXE63760.1, ECO:0000313|Proteomes:UP000290376}; RN [1] {ECO:0000313|EMBL:RXE63760.1, ECO:0000313|Proteomes:UP000290376} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate-007 (NCI) {ECO:0000313|Proteomes:UP000290376}; RA Clavel T., Strowig T.; RT "Sequence and cultivation study of Muribaculaceae reveals novel species, RT host preference, and functional potential of this yet undescribed family."; RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|HAMAP-Rule:MF_00211}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00211}; CC Note=Binds 2 magnesium ions per monomer. {ECO:0000256|HAMAP- CC Rule:MF_00211}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 2/5. {ECO:0000256|HAMAP- CC Rule:MF_00211}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00211}. CC -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase CC family. {ECO:0000256|HAMAP-Rule:MF_00211}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00211}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RXE63760.1}. 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; SCEI01000061; RXE63760.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4Q0IGA0; -. DR UniPathway; UPA00035; UER00041. DR Proteomes; UP000290376; Unassembled WGS sequence. 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; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 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 NCBIfam; TIGR01245; trpD; 1. DR PANTHER; PTHR43285; ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR43285:SF2; ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; 1. DR Pfam; PF02885; Glycos_trans_3N; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1. DR SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_00211}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00211}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00211}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00211}; Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211}. FT DOMAIN 2..63 FT /note="Glycosyl transferase family 3 N-terminal" FT /evidence="ECO:0000259|Pfam:PF02885" FT DOMAIN 72..319 FT /note="Glycosyl transferase family 3" FT /evidence="ECO:0000259|Pfam:PF00591" FT BINDING 79 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211" FT BINDING 79 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="1" FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00211" FT BINDING 91 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211" FT BINDING 107..115 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211" FT BINDING 110 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211" FT BINDING 119 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211" FT BINDING 165 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211" FT BINDING 223 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211" FT BINDING 224 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211" FT BINDING 224 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211" SQ SEQUENCE 332 AA; 36096 MW; F9662B1CCA02E9B2 CRC64; MKNILGKLIE HASLSRDEAR KVLLDIADGK CNDCQLAAFM TVYLMRSITL DELIGFRDAI LERRLPVEFD RTDAIDIVGT GGDGKNTFNI STVTCFVVAG TGRRVIKHGN YGASSVSGAS SVLEHHGVRF TTDESILRRS LDESGVCYLH APLFSPALKS VASARRQLGI RTFFNMLGPL VNPMQPRHQL LGVYSLGMMR MYHYISQYEG IECTVVHSLD GYDEISLTSP FKVAAVGGES VYRPADLGFA VVEPGELYGG DTVAEASAVF DKVLAGEGSR AQTECVLANA AFAIHTLEPH VSLLDAVEQA RESIASGRAV ECFRKFLDIN KA //