ID TRPG_SALTY Reviewed; 531 AA. AC P00905; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 08-APR-2008, entry version 86. DE Anthranilate synthase component II (EC 4.1.3.27) [Includes: Glutamine DE amidotransferase; Anthranilate phosphoribosyltransferase DE (EC 2.4.2.18)]. GN Name=trpD; Synonyms=trpGD; OrderedLocusNames=STM1724; OS Salmonella typhimurium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=602; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=84036180; 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 MEDLINE=21534948; 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 MEDLINE=81119810; 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). CC -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate + CC pyruvate + L-glutamate. CC -!- CATALYTIC ACTIVITY: N-(5-phospho-D-ribosyl)-anthranilate + CC diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1- CC diphosphate. 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: Contains 2 chains with different activities: component I CC catalyzes the formation of anthranilate using ammonia rather than CC glutamine, whereas component II provides glutamine CC amidotransferase activity. CC -!- INTERACTION: CC P00898:trpE; NbExp=1; IntAct=EBI-1030724, EBI-1030716; CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate CC phosphoribosyltransferase family. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. 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; AE008776; AAL20642.1; -; Genomic_DNA. DR EMBL; J01811; AAA57312.1; -; Genomic_DNA. DR PIR; A92907; NNEB2T. DR RefSeq; NP_460683.1; -. DR PDB; 1I1Q; X-ray; 1.90 A; B=1-193. DR PDBsum; 1I1Q; -. DR SMR; P00905; 199-530. DR IntAct; P00905; -. DR GeneID; 1253243; -. DR GenomeReviews; AE006468_GR; STM1724. DR KEGG; stm:STM1724; -. DR StyGene; SG10399; trpD. DR BioCyc; STYP99287:STM1724-MON; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR HAMAP; MF_00211; fused; 1. DR InterPro; IPR005940; Ant_phspho_trans. DR InterPro; IPR006220; Anth_synthII. DR InterPro; IPR001317; CarbamoylP_synth_GATase. DR InterPro; IPR011702; GATASE. DR InterPro; IPR000991; GATase_1. DR InterPro; IPR012998; GATase_1_AS. DR InterPro; IPR000312; Glyco_trans_3. DR InterPro; IPR006221; TrpG_papA. DR Gene3D; G3DSA:3.40.1030.10; Glyco_trans_3; 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 ProDom; PD001864; Glyco_trans_3; 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; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Complete proteome; KW Glutamine amidotransferase; Glycosyltransferase; Lyase; KW Multifunctional enzyme; Transferase; Tryptophan biosynthesis. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 531 Anthranilate synthase component II. FT /FTId=PRO_0000056897. FT DOMAIN 3 196 Glutamine amidotransferase type-1. FT REGION 202 531 Anthranilate phosphoribosyltransferase. FT ACT_SITE 84 84 For GATase activity (By similarity). FT ACT_SITE 170 170 For GATase activity (By similarity). FT ACT_SITE 172 172 For GATase activity (By similarity). FT CONFLICT 191 192 QQ -> LA (in Ref. 3; AAA57312). FT CONFLICT 511 511 V -> L (in Ref. 1; AAA27236). FT STRAND 2 7 FT HELIX 13 22 FT STRAND 26 31 FT HELIX 37 43 FT STRAND 47 53 FT HELIX 60 62 FT HELIX 66 73 FT STRAND 79 82 FT HELIX 84 92 FT STRAND 105 113 FT HELIX 117 119 FT STRAND 124 130 FT STRAND 144 149 FT STRAND 152 158 FT TURN 159 162 FT STRAND 163 169 FT HELIX 178 189 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 //