TRPD_METMA
ID TRPD_METMA Reviewed; 370 AA.
AC Q8PT97;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=MM_2820;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM32516.1; -; Genomic_DNA.
DR RefSeq; WP_011034728.1; NC_003901.1.
DR AlphaFoldDB; Q8PT97; -.
DR SMR; Q8PT97; -.
DR STRING; 192952.MM_2820; -.
DR EnsemblBacteria; AAM32516; AAM32516; MM_2820.
DR GeneID; 44087521; -.
DR GeneID; 66135219; -.
DR KEGG; mma:MM_2820; -.
DR PATRIC; fig|192952.21.peg.3255; -.
DR eggNOG; arCOG02012; Archaea.
DR HOGENOM; CLU_034315_2_1_2; -.
DR OMA; GPMTNPA; -.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000000595; 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..370
FT /note="Anthranilate phosphoribosyltransferase"
FT /id="PRO_0000154514"
FT BINDING 82
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 82
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 85..86
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 90
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 92..95
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 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 110..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 113
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 122
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 168
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
SQ SEQUENCE 370 AA; 39203 MW; 32869D152EC30EDB CRC64;
MQKIKEYIKK LEEGCDLSSE EAEAALEEVL STAEDGEIET FLLALKAKGE KPQEIVGFVR
GMKKAGNMIK PNTPFRIVDT CGTGGDGLNT INVSTAAAIV TAAAGVPVAK HGNRAATSMT
GSSDVLEALG IKVDLSPEYV RKTIEKIGIG FMFAPVFHPA MKRVAGVRKK LGVRTVFNIL
GPLTNPAGAK GQVVGVFDKN LCEPIAYALA ELGTEHALVV HGDGMDEITN TGETYVAELK
NGKVSTYTLT PESLGMLRAS PGDTKGGSPK ENARDLLCIF KGQKGPKRDL IILNAAAALY
VSGIVGSIRQ AIPIAEDAID SGKVMVKFNQ FRTFTGEFYQ IDKKQGFIPG KTALSPSRVS
MLSPASGEQA
