ID B7N476_ECOLU Unreviewed; 531 AA.
AC B7N476;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 97.
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:CAR12769.1};
GN OrderedLocusNames=ECUMN_1562 {ECO:0000313|EMBL:CAR12769.1};
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056 {ECO:0000313|EMBL:CAR12769.1, ECO:0000313|Proteomes:UP000007097};
RN [1] {ECO:0000313|Proteomes:UP000007097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC {ECO:0000313|Proteomes:UP000007097};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928163; CAR12769.1; -; Genomic_DNA.
DR RefSeq; WP_000763518.1; NC_011751.1.
DR RefSeq; YP_002412305.1; NC_011751.1.
DR AlphaFoldDB; B7N476; -.
DR STRING; 585056.ECUMN_1562; -.
DR MEROPS; C26.960; -.
DR KEGG; eum:ECUMN_1562; -.
DR PATRIC; fig|585056.7.peg.1758; -.
DR HOGENOM; CLU_014340_4_0_6; -.
DR OMA; VIYRNHV; -.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000007097; Chromosome.
DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
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; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
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 InterPro; IPR006221; TrpG/PapA_dom.
DR NCBIfam; TIGR01245; trpD; 1.
DR NCBIfam; TIGR00566; trpG_papA; 1.
DR PANTHER; PTHR43285; ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43285:SF2; ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02885; Glycos_trans_3N; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 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 Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605,
KW ECO:0000313|EMBL:CAR12769.1};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00211}; Lyase {ECO:0000313|EMBL:CAR12769.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00211};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00211};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00211};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00211}.
FT DOMAIN 5..186
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 201..263
FT /note="Glycosyl transferase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02885"
FT DOMAIN 273..521
FT /note="Glycosyl transferase family 3"
FT /evidence="ECO:0000259|Pfam:PF00591"
FT ACT_SITE 84
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 170
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 278
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 278
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 281..282
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 286
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 288..291
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 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 306..314
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 309
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 318
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 364
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 422
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
SQ SEQUENCE 531 AA; 56871 MW; 4272D79E096D4FE6 CRC64;
MADILLLDNI DSFTYNLADQ LRSNGHNVVI YRNHIPAQTL IERLATMSNP VLMLSPGPGV
PSEAGCMPEL LTRLRGKLPI IGICLGHQAI VEAYGGYVGQ AGEILHGKAS SIEHDGQAMF
AGLTNPLPVA RYHSLVGSNI PAGLTINAHF NGMVMAVRHD ADRVCGFQFH PESILTTQGA
RLLEQTLAWA QQKLEPTNTL QPILEKLYQA QTLSQQESHQ LFSAVVHGEL KPEQLAAALV
SMKIRGEHPN EIAGAATALL ENAAPFPRPD YLFADIVGTG GDGSNSINIS TASAFVAAAC
GLKVAKHGNR SVSSKSGSSD LLAAFGINLD MNADKSRQAL DELGVCFLFA PKYHTGFRHA
MSVRQQLKTR TLFNVLGPLI NPAHPPLALI GVYSPELVLP IAETLRVLGY QRAAVVHSGG
MDEVSLHAPT IVAELHDGEI KSYQLTAEDF GLTPYHQEQL AGGTPEENRD ILTRLLQGKG
DAAHEAAVAA NVAMLMRLHG HEDLQANAQT VLEVLRSGSA YDRVTALAAR G
//