ID A0A090ZDV0_PAEMA Unreviewed; 346 AA.
AC A0A090ZDV0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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:KFN09484.1};
GN ORFNames=DJ90_3189 {ECO:0000313|EMBL:KFN09484.1};
OS Paenibacillus macerans (Bacillus macerans).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=44252 {ECO:0000313|EMBL:KFN09484.1, ECO:0000313|Proteomes:UP000029278};
RN [1] {ECO:0000313|EMBL:KFN09484.1, ECO:0000313|Proteomes:UP000029278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8244 {ECO:0000313|EMBL:KFN09484.1,
RC ECO:0000313|Proteomes:UP000029278};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (APR-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFN09484.1}.
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DR EMBL; JMQA01000022; KFN09484.1; -; Genomic_DNA.
DR RefSeq; WP_036621944.1; NZ_UGSI01000001.1.
DR AlphaFoldDB; A0A090ZDV0; -.
DR STRING; 44252.DJ90_3189; -.
DR GeneID; 77006528; -.
DR PATRIC; fig|44252.3.peg.2325; -.
DR HOGENOM; CLU_034315_2_1_9; -.
DR OrthoDB; 9806430at2; -.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000029278; 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|ARBA:ARBA00023141,
KW 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:UP000029278};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00211}; Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211}.
FT DOMAIN 10..67
FT /note="Glycosyl transferase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02885"
FT DOMAIN 79..329
FT /note="Glycosyl transferase family 3"
FT /evidence="ECO:0000259|Pfam:PF00591"
FT BINDING 85
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 85
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 88..89
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..98
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 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 113..121
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 116
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 125
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 171
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
SQ SEQUENCE 346 AA; 36347 MW; D712E51AAFA1095F CRC64;
MAGQQAVQDG INRLIQGQNL GREEARGVMQ AIMNGESTPA QIGGLLTALR IKGETVEEIT
GFAEAMRGAS SRIATETSRL LDTCGTGGSG IHKINISTTA AIVAASESVR VAKHGNRSAS
GRSGSADVLE ALGVNIQLDA EQAKRCLDEI GLCFMFSQLY HPSMKHAAGP RKELGIRTVF
NMLGPLTNPA GADRQVLGIY DRTRTETIAE VLRELGSKRA LVVSSEEGLD EISLSSATRV
SELKDGVVTT YELQPEDLGL GKYPLGAMIG GDPQTNAAIV QRVLSGEKGA YRDIVLANAG
ACIYVAGLAD SIREGVAIAA AAIDSGKAYS KLEQLIRTTG ELSYVS
//
