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Database: UniProt
Entry: A0A383S7L4_9ACTN
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ID   A0A383S7L4_9ACTN        Unreviewed;       349 AA.
AC   A0A383S7L4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00211};
DE            EC=2.4.2.18 {ECO:0000256|HAMAP-Rule:MF_00211};
GN   Name=trpD {ECO:0000256|HAMAP-Rule:MF_00211,
GN   ECO:0000313|EMBL:RLP07968.1};
GN   ORFNames=D7U36_10400 {ECO:0000313|EMBL:RLP07968.1}, PROPAUS_1288
GN   {ECO:0000313|EMBL:SYZ33369.1};
OS   Propionibacterium australiense.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=119981 {ECO:0000313|EMBL:SYZ33369.1, ECO:0000313|Proteomes:UP000263928};
RN   [1] {ECO:0000313|Proteomes:UP000263928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hornung B.;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SYZ33369.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Propionibacterium_australiense1 {ECO:0000313|EMBL:SYZ33369.1};
RA   Ferrada E.E., Latorre B.A.;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:RLP07968.1, ECO:0000313|Proteomes:UP000279336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML98A078 {ECO:0000313|EMBL:RLP07968.1,
RC   ECO:0000313|Proteomes:UP000279336};
RA   Bernier A.-M., Bernard K.;
RT   "Propionibacterium australiense Genome Sequencing and Assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00211};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00211};
CC       Note=Binds 2 magnesium ions per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00211};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 2/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00211}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00211}.
CC   -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00211}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00211}.
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DR   EMBL; RCIW01000016; RLP07968.1; -; Genomic_DNA.
DR   EMBL; UNQJ01000007; SYZ33369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A383S7L4; -.
DR   OrthoDB; 9806430at2; -.
DR   UniPathway; UPA00035; UER00041.
DR   Proteomes; UP000263928; Unassembled WGS sequence.
DR   Proteomes; UP000279336; Unassembled WGS sequence.
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; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 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   NCBIfam; TIGR01245; trpD; 1.
DR   PANTHER; PTHR43285; ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43285:SF2; ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00211}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00211};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000263928};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00211}; Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211}.
FT   DOMAIN          8..69
FT                   /note="Glycosyl transferase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02885"
FT   DOMAIN          77..332
FT                   /note="Glycosyl transferase family 3"
FT                   /evidence="ECO:0000259|Pfam:PF00591"
FT   BINDING         83
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         83
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         86..87
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         91
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         93..96
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         95
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         111..119
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         114
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         123
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         169
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
SQ   SEQUENCE   349 AA;  36781 MW;  D013A33FB2BFE626 CRC64;
     MTRLTWPNLI TGLINGHDLD DEAGAWAMDQ LLSNQTSPEQ MSGFLVALRA KGETSAELSA
     LAAGMLAKAL PLELPREAVD VVGTGGDRAN TVNVSTMASI VTAASGRPVI KHGNRAASSM
     CGTAECLEAL GVVIDLSPEA EAAVFAETGI VFLFAQRYHA SMRHLAPTRR ALGVQTVFNF
     LGPLANPARP RAQALGVADE RTAPLMAQVL ADRCDRGFVF HGTDGLDEVT TTGPSDVWIL
     GGGRCERTVL DPADLGLAPA AREDLVGGDP EHNARVVHDV MAGSRGPVRD IVTLNAAAAM
     LAFDGPDFDE PIADQLRSRL EQARRVIDDG RAAALLDRWV AATRAHAGD
//
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