AC   MF_00211;
DC   Protein; auto
TR   HAMAP; MF_00211; -; 1; level=0
XX
Names: TrpD
XX
ID   TRPD
DE   RecName: Full=Anthranilate phosphoribosyltransferase;
DE            EC=2.4.2.18;
GN   Name=trpD;
XX
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).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 2 magnesium ions per monomer.;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 2/5.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC       family.
XX
DR   Pfam; PF00591; Glycos_transf_3; 1; trigger=no
DR   Pfam; PF02885; Glycos_trans_3N; 1; trigger=no
DR   NCBIfam; TIGR01245; TrpD; 1; trigger=no
XX
KW   Amino-acid biosynthesis
KW   Aromatic amino acid biosynthesis
KW   Tryptophan biosynthesis
KW   Transferase
KW   Glycosyltransferase
KW   Magnesium
KW   Metal-binding
XX
GO   GO:0000287; F:magnesium ion binding
GO   GO:0004048; F:anthranilate phosphoribosyltransferase activity
GO   GO:0000162; P:tryptophan biosynthetic process
XX
FT   From: TRPD_MYCTU (P9WFX5)
FT   BINDING         110..111
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Optional; Condition: G-[DSN]
FT   BINDING         117..120
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Optional; Condition: N-x-[ST]-[TS]
FT   BINDING         135..143
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Optional; Condition: K-x(2)-[NGAS]-x(3)-[TSV]-[SG]
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: [ST]
FT   BINDING         251
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         107
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Condition: G
FT   BINDING         115
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Condition: [TS]
FT   BINDING         147
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Condition: [GA]
FT   From: TRPD_SACS2 (P50384)
FT   BINDING         79
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT   Condition: G
FT   BINDING         109
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT   Condition: N
FT   BINDING         118
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Condition: [ST]
FT   BINDING         164
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="2"
FT   Condition: R
XX
Size: 320-370;
Related: None;
Template: P50384; P9WFX5;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: MF_00134 (trpC); <glutamine amidotransferase type-1 domain>
 Cter: None
Duplicate: in NOSS1, RALN1, STRCO
Plasmid: None
Comments: There are divergent trpD-like proteins in AQUAE (O66585) and ECOLI (P30177)
XX
# Revision 1.40 2023/11/28
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