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TRPD_SULIN
ID   TRPD_SULIN              Reviewed;         345 AA.
AC   C3NHL1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00211};
DE            EC=2.4.2.18 {ECO:0000255|HAMAP-Rule:MF_00211};
GN   Name=trpD {ECO:0000255|HAMAP-Rule:MF_00211}; OrderedLocusNames=YN1551_1533;
OS   Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=419942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.N.15.51 / Yellowstone #2;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(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:0000255|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:0000255|HAMAP-Rule:MF_00211};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00211};
CC       Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP-
CC       Rule:MF_00211};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 2/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00211}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00211}.
CC   -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00211}.
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DR   EMBL; CP001404; ACP48621.1; -; Genomic_DNA.
DR   RefSeq; WP_012717485.1; NC_012623.1.
DR   AlphaFoldDB; C3NHL1; -.
DR   SMR; C3NHL1; -.
DR   EnsemblBacteria; ACP48621; ACP48621; YN1551_1533.
DR   GeneID; 7809124; -.
DR   KEGG; sin:YN1551_1533; -.
DR   HOGENOM; CLU_034315_2_1_2; -.
DR   OMA; GPMTNPA; -.
DR   UniPathway; UPA00035; UER00041.
DR   Proteomes; UP000006818; Chromosome.
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; -; 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   PANTHER; PTHR43285; PTHR43285; 1.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   SUPFAM; SSF47648; SSF47648; 1.
DR   SUPFAM; SSF52418; SSF52418; 1.
DR   TIGRFAMs; TIGR01245; trpD; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Glycosyltransferase; Magnesium; Metal-binding; Transferase;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..345
FT                   /note="Anthranilate phosphoribosyltransferase"
FT                   /id="PRO_1000204193"
FT   BINDING         79
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         79
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         82..83
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         87
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         89..92
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         91
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         106..114
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         109
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         118
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         164
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
SQ   SEQUENCE   345 AA;  37608 MW;  05BE38BF1A738C8A CRC64;
     MNINDILKKL INKSDLEIDE AEELAKAIIR GEVPEILVSA ILVALRMKGE SKNEIVGFAR
     AMRELAIKID VPNAIDTAGT GGDGLGTVNV STASAILLSL INPVAKHGNR AVSGKSGSAD
     VLEALGYNII VPPERAKELI HKTNFVFLFA QYYHPAMKNV ANVRKTLGIR TIFNILGPLT
     NPANAKYQLM GVFSKDHLDL LSKSAYELDF NKVILVHGEP GIDEVSPIGK TFMKIVSKRG
     IEEVKFDVTD FGISSIPIDK LIVNSAEDSA IKIVRAFLGK DEHVAEFIKI NTAVALFALD
     KVSNFKEGYE YAKYLIENSV NKLNEIISLN GDLTKLKTIM VKSSG
 
 
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