TRPD_PAEAT
ID TRPD_PAEAT Reviewed; 352 AA.
AC A1R6T5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=AAur_2206;
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=290340;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1;
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(2006).
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; CP000474; ABM09784.1; -; Genomic_DNA.
DR RefSeq; WP_011774891.1; NC_008711.1.
DR AlphaFoldDB; A1R6T5; -.
DR SMR; A1R6T5; -.
DR STRING; 290340.AAur_2206; -.
DR EnsemblBacteria; ABM09784; ABM09784; AAur_2206.
DR KEGG; aau:AAur_2206; -.
DR eggNOG; COG0547; Bacteria.
DR HOGENOM; CLU_034315_4_1_11; -.
DR OMA; GPMTNPA; -.
DR OrthoDB; 1238435at2; -.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000000637; 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..352
FT /note="Anthranilate phosphoribosyltransferase"
FT /id="PRO_0000325412"
FT BINDING 91
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 91
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 94..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 99
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 101..104
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 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 119..127
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 122
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 131
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 177
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
SQ SEQUENCE 352 AA; 36229 MW; B0FF42014F142BF8 CRC64;
MTSPASAPAA SNTWPGLISA LINGDDLAVG NTEWAMNTIM AGEATPAQIA GFLVALRAKG
ETVEELAGLV EAMVQHANPI DISGEKLDIV GTGGDRLNTV NISTMAALVA AGAGAKVVKH
GNRAASSASG SADVLEALGV RLDLSIEQVA RNAEEAGITF CFAQVFHPSF RHTAVPRREL
AVPTAFNFLG PMTNPAHVQA SAVGVANARM APLVAGVLAR RGSRGLVFRG DDGLDELTPT
GPSTVWEFRN GTVKEQVFTP ADLGIRPSTV ADLRGGDAAA NAAVVREILD GKTGPVRDAV
LLNAAAGLVS IDLHAEGSLE QRMRTAFARA AESVDSGKAA EVLAKWTALS QS
