ID TRPD_MYCPA Reviewed; 367 AA. AC Q73YM4; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 26-FEB-2020, entry version 98. 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=MAP_1931c; OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10) OS (Mycobacterium paratuberculosis). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium avium complex (MAC). OX NCBI_TaxID=262316; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-968 / K-10; RX PubMed=16116077; DOI=10.1073/pnas.0505662102; RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., RA Kanjilal S., Kapur V.; RT "The complete genome sequence of Mycobacterium avium subspecies RT paratuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(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; AE016958; AAS04248.1; -; Genomic_DNA. DR SMR; Q73YM4; -. DR STRING; 262316.MAP_1931c; -. DR PRIDE; Q73YM4; -. DR EnsemblBacteria; AAS04248; AAS04248; MAP_1931c. DR KEGG; mpa:MAP_1931c; -. DR eggNOG; ENOG4108I0Q; Bacteria. DR eggNOG; COG0547; LUCA. DR HOGENOM; CLU_034315_4_1_11; -. DR KO; K00766; -. DR OMA; HHSAMKH; -. DR UniPathway; UPA00035; UER00041. DR Proteomes; UP000000580; 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; 1.20.970.10; -; 1. 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 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..367 FT /note="Anthranilate phosphoribosyltransferase" FT /id="PRO_0000227169" FT REGION 107..108 FT /note="Phosphoribosylpyrophosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT REGION 114..117 FT /note="Phosphoribosylpyrophosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT REGION 132..140 FT /note="Phosphoribosylpyrophosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT METAL 116 FT /note="Magnesium 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT METAL 248 FT /note="Magnesium 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT METAL 249 FT /note="Magnesium 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT METAL 249 FT /note="Magnesium 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 104 FT /note="Anthranilate 1; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 104 FT /note="Phosphoribosylpyrophosphate; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 112 FT /note="Phosphoribosylpyrophosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 135 FT /note="Anthranilate 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 144 FT /note="Phosphoribosylpyrophosphate; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 190 FT /note="Anthranilate 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" SQ SEQUENCE 367 AA; 37729 MW; 05F73559DB6DAEFE CRC64; MALSSESSAA SAARRPSGGP ATSWRQVLAR LTGGDDLARG QAAWAMDQIM TGEASPAQIA AFAVAMQVKV PTSAEVIELA EVMLNHALPF PAGAIRDDTV DIVGTGGDGV NTLNLSTMAA IVAAAAGVPV VKHGNRAASS LSGGADTLEE LGVRIDLGPE QVARSVAEVG IGFCFAPLFH PSYRHTSAVR REIGVPTVFN LLGPLTNPAR PRAGLIGCAF AELAEVMAGV FAARRSSVLV VHGDDGLDEL TTTTTSTIWR VQAGTVDRLT FDPAGFGFPR AELDDLLGGD AQTNAAEVRA VLAGGQGPVR DAVVLNAAGA IVAHAGLSSR AEWLPAWEDG LARASAAIDS GAAEQLLARW VRFGQQL //