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 24-JUN-2015, entry version 76. 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}; GN OrderedLocusNames=MAP_1931c; OS Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10). 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., RA Banerji N., 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 CC N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000255|HAMAP- CC Rule:MF_00211}. CC -!- CATALYTIC ACTIVITY: N-(5-phospho-D-ribosyl)-anthranilate + CC diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1- CC diphosphate. {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 RefSeq; NP_960865.1; NC_002944.2. DR RefSeq; WP_010949417.1; NC_002944.2. DR ProteinModelPortal; Q73YM4; -. DR SMR; Q73YM4; 23-367. DR STRING; 262316.MAP1931c; -. DR EnsemblBacteria; AAS04248; AAS04248; MAP_1931c. DR KEGG; mpa:MAP1931c; -. DR PATRIC; 17996442; VBIMycAvi108102_2048. DR eggNOG; COG0547; -. DR KO; K00766; -. DR OMA; RVWTVHG; -. DR OrthoDB; EOG6D5G6B; -. DR BioCyc; MAVI262316:GCQR-1954-MONOMER; -. DR UniPathway; UPA00035; UER00041. DR Proteomes; UP000000580; Chromosome. DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-HAMAP. 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 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 Complete proteome; Glycosyltransferase; Magnesium; Metal-binding; KW Reference proteome; Transferase; Tryptophan biosynthesis. FT CHAIN 1 367 Anthranilate phosphoribosyltransferase. FT /FTId=PRO_0000227169. FT REGION 107 108 Phosphoribosylpyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT REGION 114 117 Phosphoribosylpyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT REGION 132 140 Phosphoribosylpyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT METAL 116 116 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT METAL 248 248 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT METAL 249 249 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT METAL 249 249 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 104 104 Anthranilate 1; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT BINDING 104 104 Phosphoribosylpyrophosphate; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 112 112 Phosphoribosylpyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT BINDING 135 135 Anthranilate 1. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 144 144 Phosphoribosylpyrophosphate; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 190 190 Anthranilate 2. {ECO:0000255|HAMAP- FT 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 //