ID A0A4Q0IGA0_9BACT Unreviewed; 332 AA. AC A0A4Q0IGA0; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 18-SEP-2019, entry version 2. DE RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS01090345}; DE EC=2.4.2.18 {ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS01090347}; 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; Bacteroidetes; 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 RT species, host preference, and functional potential of this yet RT 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 CC N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000256|HAMAP- CC Rule:MF_00211, ECO:0000256|SAAS:SAAS00918330}. CC -!- CATALYTIC ACTIVITY: CC Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = CC 5-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 ECO:0000256|SAAS:SAAS01124167}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC 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, ECO:0000256|SAAS:SAAS00083106}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00211, CC ECO:0000256|SAAS:SAAS00918319}. CC -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase CC family. {ECO:0000256|HAMAP-Rule:MF_00211, CC ECO:0000256|SAAS:SAAS01090338}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00211}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 UniPathway; UPA00035; UER00041. DR Proteomes; UP000290376; Unassembled WGS sequence. 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 {ECO:0000256|HAMAP-Rule:MF_00211, KW ECO:0000256|SAAS:SAAS00458438}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211, KW ECO:0000256|SAAS:SAAS00458470}; KW Complete proteome {ECO:0000313|Proteomes:UP000290376}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00211, KW ECO:0000256|SAAS:SAAS00083140, ECO:0000313|EMBL:RXE63760.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00211, KW ECO:0000256|SAAS:SAAS00918354}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00211, KW ECO:0000256|SAAS:SAAS00918356}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00211, KW ECO:0000256|SAAS:SAAS00458476, ECO:0000313|EMBL:RXE63760.1}; KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211, KW ECO:0000256|SAAS:SAAS00458450}. FT DOMAIN 3 62 Glycos_trans_3N. {ECO:0000259|Pfam: FT PF02885}. FT DOMAIN 72 319 Glycos_transf_3. {ECO:0000259|Pfam: FT PF00591}. FT REGION 82 83 Phosphoribosylpyrophosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00211}. FT REGION 89 92 Phosphoribosylpyrophosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00211}. FT REGION 107 115 Phosphoribosylpyrophosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00211}. FT METAL 91 91 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_00211}. FT METAL 223 223 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00211}. FT METAL 224 224 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_00211}. FT METAL 224 224 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00211}. FT BINDING 79 79 Anthranilate 1; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00211}. FT BINDING 79 79 Phosphoribosylpyrophosphate; via amide FT nitrogen. {ECO:0000256|HAMAP-Rule: FT MF_00211}. FT BINDING 87 87 Phosphoribosylpyrophosphate. FT {ECO:0000256|HAMAP-Rule:MF_00211}. FT BINDING 110 110 Anthranilate 1. {ECO:0000256|HAMAP-Rule: FT MF_00211}. FT BINDING 119 119 Phosphoribosylpyrophosphate; via amide FT nitrogen. {ECO:0000256|HAMAP-Rule: FT MF_00211}. FT BINDING 165 165 Anthranilate 2. {ECO:0000256|HAMAP-Rule: FT 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 //