HAMAP logo

HAMAP rule MF_00211

Send feedback

General rule information [?]

Accession MF_00211
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 39)
Name TrpD
Scope(s) Bacteria
Archaea
Template(s) P50384 (TRPD_SACS2); P9WFX5 (TRPD_MYCTU); [ Recover all ]
Triggered by HAMAP; MF_00211 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier TRPD
Protein name RecName: Full=Anthranilate phosphoribosyltransferase;
                 EC=2.4.2.18;
Gene name Name=trpD;

Comments [?]

FUNCTIONCatalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA).
CATALYTIC ACTIVITY Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5- phospho-alpha-D-ribose 1-diphosphate + anthranilate; Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18;
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions per monomer.;
PATHWAYAmino-acid biosynthesis; L-tryptophan biosynthesis; L- tryptophan from chorismate: step 2/5.
SUBUNITHomodimer.
SIMILARITYBelongs to the anthranilate phosphoribosyltransferase family.

Keywords [?]


Gene Ontology [?]

GO:0000287; Molecular function:magnesium ion binding
GO:0004048; Molecular function:anthranilate phosphoribosyltransferase activity
GO:0000162; Biological process:tryptophan biosynthetic process

Cross-references [?]

Pfam PF00591; Glycos_transf_3; 1;
Pfam PF02885; Glycos_trans_3N; 1;
NCBIfam TIGR01245; TrpD; 1;

Features [?]

From: TRPD_MYCTU (P9WFX5)
Key From To Description Tag Condition FTGroup
BINDING 110 111 /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
/ligand_id="ChEBI:CHEBI:58017"
G-[DSN]
BINDING 117 120 /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
/ligand_id="ChEBI:CHEBI:58017"
N-x-[ST]-[TS]
BINDING 135 143 /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
/ligand_id="ChEBI:CHEBI:58017"
K-x(2)-[NGAS]-x(3)-[TSV]-[SG]
BINDING 119 119 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="1"
[ST]
BINDING 251 251 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="2"
D
BINDING 252 252 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="1"
E
BINDING 252 252 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="2"
E
BINDING 107 107 /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
/ligand_id="ChEBI:CHEBI:58017"
G
BINDING 115 115 /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
/ligand_id="ChEBI:CHEBI:58017"
[TS]
BINDING 147 147 /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
/ligand_id="ChEBI:CHEBI:58017"
[GA]
From: TRPD_SACS2 (P50384)
Key From To Description Tag Condition FTGroup
BINDING 79 79 /ligand="anthranilate"
/ligand_id="ChEBI:CHEBI:16567"
/ligand_label="1"
G
BINDING 109 109 /ligand="anthranilate"
/ligand_id="ChEBI:CHEBI:16567"
/ligand_label="1"
N
BINDING 118 118 /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
/ligand_id="ChEBI:CHEBI:58017"
[ST]
BINDING 164 164 /ligand="anthranilate"
/ligand_id="ChEBI:CHEBI:16567"
/ligand_label="2"
R

Additional information [?]

Size range 320-370 amino acids
Related rules None
Fusion Nter: MF_00134 (trpC); <glutamine amidotransferase type-1 domain> Cter: None
Comments There are divergent trpD-like proteins in AQUAE (O66585) and ECOLI (P30177)



View rule in raw text format (no links)