TRPD_FRATW
ID TRPD_FRATW Reviewed; 337 AA.
AC A4J0E5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 84.
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=FTW_2023;
OS Francisella tularensis subsp. tularensis (strain WY96-3418).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=418136;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WY96-3418;
RX PubMed=17895988; DOI=10.1371/journal.pone.0000947;
RA Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V.,
RA Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D.,
RA Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J.,
RA Wagner D.M., Brettin T.S., Brown N., Gilna P., Keim P.S.;
RT "Complete genomic characterization of a pathogenic A.II strain of
RT Francisella tularensis subspecies tularensis.";
RL PLoS ONE 2:E947-E947(2007).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABO47647.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000608; ABO47647.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003027659.1; NC_009257.1.
DR AlphaFoldDB; A4J0E5; -.
DR SMR; A4J0E5; -.
DR KEGG; ftw:FTW_2023; -.
DR HOGENOM; CLU_034315_3_0_6; -.
DR UniPathway; UPA00035; UER00041.
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; Transferase;
KW Tryptophan biosynthesis.
FT CHAIN 1..337
FT /note="Anthranilate phosphoribosyltransferase"
FT /id="PRO_0000325427"
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 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 337 AA; 37147 MW; D4EE76380B6A302F CRC64;
MISLKSIVDK LYNLEDLSYQ ESYQLFDYFI KGQIELPLQT SILTALKLKK ETSIEIAAAV
EALFDNTKEF PKIKGDLAGI VGTGGDGFNT INISTTAAIV AATAGYKVAK HGGRSVSSKS
GSFDLLESFG VNIELAPDQT KQCLELYNLG FLFVPFYSDG FRHIKEARTI LKTRTIFNIL
GPLINPARPN KVVIGVYSKD LILPMAKTLV NLGIDRAVVV YGSGLDEVAI HDDTYVAEIQ
NNQIIEYKVS PVDFGIDTYA IKDLEGGLPE QNREIIKQIL LGKGKEAHNA AVAVNVAMLM
KLYDKDDLKQ NTQEVLEIIK SGKCFNILQQ VINYSNK
