ID TRPGD_SALTY Reviewed; 531 AA. AC P00905; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 24-JUL-2024, entry version 191. DE RecName: Full=Bifunctional protein TrpGD; DE Includes: DE RecName: Full=Anthranilate synthase component 2; DE Short=AS; DE Short=ASII; DE EC=4.1.3.27; DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component; DE Includes: DE RecName: Full=Anthranilate phosphoribosyltransferase; DE EC=2.4.2.18; GN Name=trpGD; Synonyms=trpD; OrderedLocusNames=STM1724; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6355484; DOI=10.1016/s0022-2836(83)80136-3; RA Horowitz H., van Arsdell J., Platt T.; RT "Nucleotide sequence of the trpD and trpC genes of Salmonella RT typhimurium."; RL J. Mol. Biol. 169:775-797(1983). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201. RX PubMed=7007652; DOI=10.1016/0022-2836(80)90260-0; RA Nichols B.P., Miozzari G.F., van Cleemput M., Bennett G.N., Yanofsky C.; RT "Nucleotide sequences of the trpG regions of Escherichia coli, Shigella RT dysenteriae, Salmonella typhimurium and Serratia marcescens."; RL J. Mol. Biol. 142:503-517(1980). RN [4] RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT. RX PubMed=4914739; DOI=10.1016/s0021-9258(18)63027-3; RA Nagano H., Zalkin H.; RT "Some physicochemical properties of anthranilate synthetase component I RT from Salmonella typhimurium."; RL J. Biol. Chem. 245:3097-3103(1970). RN [5] RP ACTIVITY REGULATION. RX PubMed=2022650; DOI=10.1016/s0021-9258(18)92979-0; RA Caligiuri M.G., Bauerle R.; RT "Identification of amino acid residues involved in feedback regulation of RT the anthranilate synthase complex from Salmonella typhimurium. Evidence for RT an amino-terminal regulatory site."; RL J. Biol. Chem. 266:8328-8335(1991). RN [6] RP CRYSTALLIZATION, AND SUBUNIT. RX PubMed=10089433; DOI=10.1107/s0907444998010233; RA Tolbert W.D., Chatterji S., Bauerle R., Kretsinger R.; RT "Crystallization and preliminary crystallographic studies of the RT anthranilate synthase partial complex from Salmonella typhimurium."; RL Acta Crystallogr. D 55:305-306(1999). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT. RX PubMed=11224570; DOI=10.1038/84988; RA Morollo A.A., Eck M.J.; RT "Structure of the cooperative allosteric anthranilate synthase from RT Salmonella typhimurium."; RL Nat. Struct. Biol. 8:243-247(2001). CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two- CC step biosynthesis of anthranilate, an intermediate in the biosynthesis CC of L-tryptophan. In the first step, the glutamine-binding beta subunit CC (TrpG) of anthranilate synthase (AS) provides the glutamine CC amidotransferase activity which generates ammonia as a substrate that, CC along with chorismate, is used in the second step, catalyzed by the CC large alpha subunit of AS (TrpE) to produce anthranilate. In the CC absence of TrpG, TrpE can synthesize anthranilate directly from CC chorismate and high concentrations of ammonia. In addition to CC synthesizing anthranilate, it also catalyzes the second step of the CC pathway, the transfer of the phosphoribosyl group of 5- CC phosphorylribose-1-pyrophosphate (PRPP) to anthranilate. CC {ECO:0000269|PubMed:4914739}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:58359; EC=4.1.3.27; 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 -!- ACTIVITY REGULATION: Cooperatively feedback inhibited by tryptophan. CC {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4914739}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 2/5. CC -!- SUBUNIT: Monomer. Heterotetramer consisting of two non-identical CC subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE) CC (Probable). {ECO:0000305|PubMed:10089433, ECO:0000305|PubMed:11224570, CC ECO:0000305|PubMed:4914739}. CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate CC phosphoribosyltransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AH000942; AAA27236.1; -; Genomic_DNA. DR EMBL; AE006468; AAL20642.1; -; Genomic_DNA. DR EMBL; J01811; AAA57312.1; -; Genomic_DNA. DR PIR; A92907; NNEB2T. DR RefSeq; NP_460683.1; NC_003197.2. DR RefSeq; WP_000763494.1; NC_003197.2. DR PDB; 1I1Q; X-ray; 1.90 A; B=2-193. DR PDBsum; 1I1Q; -. DR AlphaFoldDB; P00905; -. DR SMR; P00905; -. DR IntAct; P00905; 1. DR MINT; P00905; -. DR STRING; 99287.STM1724; -. DR MEROPS; C26.960; -. DR PaxDb; 99287-STM1724; -. DR GeneID; 1253243; -. DR KEGG; stm:STM1724; -. DR PATRIC; fig|99287.12.peg.1820; -. DR HOGENOM; CLU_014340_4_0_6; -. DR PhylomeDB; P00905; -. DR BioCyc; SENT99287:STM1724-MONOMER; -. DR SABIO-RK; P00905; -. DR UniPathway; UPA00035; UER00040. DR UniPathway; UPA00035; UER00041. DR EvolutionaryTrace; P00905; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IBA:GO_Central. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0002047; P:phenazine biosynthetic process; IBA:GO_Central. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Glutamine amidotransferase; KW Glycosyltransferase; Lyase; Multifunctional enzyme; Reference proteome; KW Transferase; Tryptophan biosynthesis. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..531 FT /note="Bifunctional protein TrpGD" FT /id="PRO_0000056897" FT DOMAIN 3..196 FT /note="Glutamine amidotransferase type-1" FT REGION 202..531 FT /note="Anthranilate phosphoribosyltransferase" FT ACT_SITE 84 FT /note="Nucleophile; for GATase activity" FT /evidence="ECO:0000250|UniProtKB:P00900" FT ACT_SITE 170 FT /note="For GATase activity" FT /evidence="ECO:0000250" FT ACT_SITE 172 FT /note="For GATase activity" FT /evidence="ECO:0000250" FT BINDING 57..59 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT BINDING 88 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT BINDING 134..135 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT CONFLICT 191..192 FT /note="QQ -> LA (in Ref. 3; AAA57312)" FT /evidence="ECO:0000305" FT CONFLICT 511 FT /note="V -> L (in Ref. 1; AAA27236)" FT /evidence="ECO:0000305" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:1I1Q" FT HELIX 14..23 FT /evidence="ECO:0007829|PDB:1I1Q" FT STRAND 27..32 FT /evidence="ECO:0007829|PDB:1I1Q" FT HELIX 38..44 FT /evidence="ECO:0007829|PDB:1I1Q" FT STRAND 48..54 FT /evidence="ECO:0007829|PDB:1I1Q" FT HELIX 61..63 FT /evidence="ECO:0007829|PDB:1I1Q" FT HELIX 67..74 FT /evidence="ECO:0007829|PDB:1I1Q" FT STRAND 80..83 FT /evidence="ECO:0007829|PDB:1I1Q" FT HELIX 85..93 FT /evidence="ECO:0007829|PDB:1I1Q" FT STRAND 106..114 FT /evidence="ECO:0007829|PDB:1I1Q" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:1I1Q" FT STRAND 125..131 FT /evidence="ECO:0007829|PDB:1I1Q" FT STRAND 145..150 FT /evidence="ECO:0007829|PDB:1I1Q" FT STRAND 153..159 FT /evidence="ECO:0007829|PDB:1I1Q" FT TURN 160..163 FT /evidence="ECO:0007829|PDB:1I1Q" FT STRAND 164..170 FT /evidence="ECO:0007829|PDB:1I1Q" FT HELIX 179..190 FT /evidence="ECO:0007829|PDB:1I1Q" SQ SEQUENCE 531 AA; 56918 MW; 256D2409062CD4C7 CRC64; MADILLLDNI DSFTWNLADQ LRTNGHNVVI YRNHIPAQTL IDRLATMKNP VLMLSPGPGV PSEAGCMPEL LTRLRGKLPI IGICLGHQAI VEAYGGYVGQ AGEILHGKAS SIEHDGQAMF AGLANPLPVA RYHSLVGSNV PAGLTINAHF NGMVMAVRHD ADRVCGFQFH PESILTTQGA RLLEQTLAWA QQKLEPTNTL QPILEKLYQA QTLTQQESHQ LFSAVVRGEL KPEQLAAALV SMKIRGEHPN EIAGAATALL ENAAPFPRPE YLFADIVGTG GDGSNSINIS TASAFVAAAC GLKVAKHGNR SVSSKSGSSD LLAAFGINLD MNADKSRQAL DELGVCFLFA PKYHTGLRHA MPVRQQLKTR TLFNVLGPLI NPAHPPLALI GVYSPELVLP IAETLRVLGY QRAAVVHSGG MDEVSLHAPT IVAELHDGEI KSYQLTAEDF GLTPYHQDQL AGGTPEENRD ILTRLLQGKG DAAHEAAVAA NVAMLMRLHG QEDLKANAQT VLDVLRNGTA YDRVTALAAR G //