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 18-SEP-2019, entry version 167. 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; Proteobacteria; 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., RA Waterston R., Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium RT 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., RA Yanofsky C.; RT "Nucleotide sequences of the trpG regions of Escherichia coli, RT Shigella dysenteriae, Salmonella typhimurium and Serratia RT marcescens."; RL J. Mol. Biol. 142:503-517(1980). RN [4] RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT. RX PubMed=4914739; RA Nagano H., Zalkin H.; RT "Some physicochemical properties of anthranilate synthetase component RT I from Salmonella typhimurium."; RL J. Biol. Chem. 245:3097-3103(1970). RN [5] RP ACTIVITY REGULATION. RX PubMed=2022650; RA Caligiuri M.G., Bauerle R.; RT "Identification of amino acid residues involved in feedback regulation RT of the anthranilate synthase complex from Salmonella typhimurium. RT Evidence for 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 CC two-step biosynthesis of anthranilate, an intermediate in the CC biosynthesis of L-tryptophan. In the first step, the glutamine- CC binding beta subunit (TrpG) of anthranilate synthase (AS) provides CC the glutamine amidotransferase activity which generates ammonia as CC a substrate that, along with chorismate, is used in the second CC step, catalyzed by the large alpha subunit of AS (TrpE) to produce CC anthranilate. In the absence of TrpG, TrpE can synthesize CC anthranilate directly from chorismate and high concentrations of CC ammonia. In addition to synthesizing anthranilate, it also CC catalyzes the second step of the pathway, the transfer of the CC phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) CC to anthranilate. {ECO:0000269|PubMed:4914739}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L- CC glutamate + pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27; CC -!- CATALYTIC ACTIVITY: CC Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = CC 5-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 CC tryptophan. {ECO:0000269|PubMed:2022650, CC 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, CC ECO:0000305|PubMed:11224570, 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; M30285; 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 SMR; P00905; -. DR IntAct; P00905; 1. DR MINT; P00905; -. DR MEROPS; C26.960; -. DR PaxDb; P00905; -. DR PRIDE; P00905; -. DR EnsemblBacteria; AAL20642; AAL20642; STM1724. DR GeneID; 1253243; -. DR KEGG; stm:STM1724; -. DR PATRIC; fig|99287.12.peg.1820; -. DR eggNOG; ENOG4108EFP; Bacteria. DR eggNOG; COG0512; LUCA. DR eggNOG; COG0547; LUCA. DR HOGENOM; HOG000230451; -. DR KO; K13497; -. DR OMA; KCFNTLQ; -. 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 Gene3D; 3.40.1030.10; -; 1. DR Gene3D; 3.40.50.880; -; 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 Pfam; PF00117; GATase; 1. DR Pfam; PF02885; Glycos_trans_3N; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR SUPFAM; SSF47648; SSF47648; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF52418; SSF52418; 1. DR TIGRFAMs; TIGR01245; trpD; 1. DR TIGRFAMs; TIGR00566; trpG_papA; 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; Complete proteome; KW Glutamine amidotransferase; Glycosyltransferase; Lyase; KW Multifunctional enzyme; Reference proteome; Transferase; KW Tryptophan biosynthesis. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 531 Bifunctional protein TrpGD. FT /FTId=PRO_0000056897. FT DOMAIN 3 196 Glutamine amidotransferase type-1. FT REGION 57 59 Glutamine binding. FT {ECO:0000250|UniProtKB:P00900}. FT REGION 134 135 Glutamine binding. FT {ECO:0000250|UniProtKB:P00900}. FT REGION 202 531 Anthranilate phosphoribosyltransferase. FT ACT_SITE 84 84 Nucleophile; for GATase activity. FT {ECO:0000250|UniProtKB:P00900}. FT ACT_SITE 170 170 For GATase activity. {ECO:0000250}. FT ACT_SITE 172 172 For GATase activity. {ECO:0000250}. FT BINDING 88 88 Glutamine. FT {ECO:0000250|UniProtKB:P00900}. FT CONFLICT 191 192 QQ -> LA (in Ref. 3; AAA57312). FT {ECO:0000305}. FT CONFLICT 511 511 V -> L (in Ref. 1; AAA27236). FT {ECO:0000305}. FT STRAND 3 8 {ECO:0000244|PDB:1I1Q}. FT HELIX 14 23 {ECO:0000244|PDB:1I1Q}. FT STRAND 27 32 {ECO:0000244|PDB:1I1Q}. FT HELIX 38 44 {ECO:0000244|PDB:1I1Q}. FT STRAND 48 54 {ECO:0000244|PDB:1I1Q}. FT HELIX 61 63 {ECO:0000244|PDB:1I1Q}. FT HELIX 67 74 {ECO:0000244|PDB:1I1Q}. FT STRAND 80 83 {ECO:0000244|PDB:1I1Q}. FT HELIX 85 93 {ECO:0000244|PDB:1I1Q}. FT STRAND 106 114 {ECO:0000244|PDB:1I1Q}. FT HELIX 118 120 {ECO:0000244|PDB:1I1Q}. FT STRAND 125 131 {ECO:0000244|PDB:1I1Q}. FT STRAND 145 150 {ECO:0000244|PDB:1I1Q}. FT STRAND 153 159 {ECO:0000244|PDB:1I1Q}. FT TURN 160 163 {ECO:0000244|PDB:1I1Q}. FT STRAND 164 170 {ECO:0000244|PDB:1I1Q}. FT HELIX 179 190 {ECO:0000244|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 //