ID TRPG_SALTY STANDARD; PRT; 530 AA. AC P00905; DT 21-JUL-1986 (Rel. 01, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Anthranilate synthase component II (EC 4.1.3.27) [Includes: Glutamine DE amidotransferase; Anthranilate phosphoribosyltransferase DE (EC 2.4.2.18)]. GN TRPD OR TRPGD OR STM1724. OS Salmonella typhimurium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=602; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=84036180; PubMed=6355484; 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 SEQUENCE FROM N.A. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX MEDLINE=21534948; PubMed=11677609; 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 SEQUENCE OF 1-200 FROM N.A. RX MEDLINE=81119810; PubMed=7007652; 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: Anthranilate + phosphoribosylpyrophosphate = CC N-5'-phosphoribosyl-anthranilate + diphosphate. CC -!- PATHWAY: Tryptophan biosynthesis; first step. CC -!- PATHWAY: Tryptophan biosynthesis; second step. CC -!- SUBUNIT: CONTAINS 2 CHAINS WITH DIFFERENT ACTIVITIES: COMPONENT 1 CC CATALYZES THE FORMATION OF ANTHRANILATE USING AMMONIA RATHER THAN CC GLUTAMINE, WHEREAS COMPONENT 2 PROVIDES GLUTAMINE AMIDOTRANSFERASE CC ACTIVITY. CC -!- SIMILARITY: Contains 1 type-1 glutamine amidotransferase domain. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE ANTHRANILATE CC PHOSPHORIBOSYLTRANSFERASE FAMILY. 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; -. DR EMBL; AE008776; AAL20642.1; -. DR EMBL; J01811; AAA57312.1; -. DR PIR; A01126; NNEB2T. DR HSSP; Q06129; 1QDL. DR StyGene; SG10399; trpD. DR HAMAP; MF_00211; fused; 1. DR InterPro; IPR005940; Ant_phspho_trans. DR InterPro; IPR006220; Anth_synthII. DR InterPro; IPR001317; CPS_GATase. DR InterPro; IPR000991; GATase_1. DR InterPro; IPR000312; Glyco_trans_3. DR InterPro; IPR006221; TrpG_papA. DR Pfam; PF00117; GATase; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR Pfam; PF02885; Glycos_trans_3N; 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; PS00442; GATASE_TYPE_I; 1. KW Tryptophan biosynthesis; Lyase; Transferase; Glycosyltransferase; KW Multifunctional enzyme; Glutamine amidotransferase; Complete proteome. FT INIT_MET 0 0 BY SIMILARITY. FT DOMAIN 1 200 GLUTAMINE AMIDOTRANSFERASE. FT DOMAIN 201 530 ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE. FT ACT_SITE 83 83 GATASE (BY SIMILARITY). FT ACT_SITE 169 169 GATASE (BY SIMILARITY). FT ACT_SITE 171 171 GATASE (BY SIMILARITY). FT CONFLICT 190 191 QQ -> LA (IN REF. 3). FT CONFLICT 510 510 V -> L (IN REF. 1). SQ SEQUENCE 530 AA; 56787 MW; 256D30FE2127E4C7 CRC64; ADILLLDNID SFTWNLADQL RTNGHNVVIY RNHIPAQTLI DRLATMKNPV LMLSPGPGVP SEAGCMPELL TRLRGKLPII GICLGHQAIV EAYGGYVGQA GEILHGKASS IEHDGQAMFA GLANPLPVAR YHSLVGSNVP AGLTINAHFN GMVMAVRHDA DRVCGFQFHP ESILTTQGAR LLEQTLAWAQ QKLEPTNTLQ PILEKLYQAQ TLTQQESHQL FSAVVRGELK PEQLAAALVS MKIRGEHPNE IAGAATALLE NAAPFPRPEY LFADIVGTGG DGSNSINIST ASAFVAAACG LKVAKHGNRS VSSKSGSSDL LAAFGINLDM NADKSRQALD ELGVCFLFAP KYHTGLRHAM PVRQQLKTRT LFNVLGPLIN PAHPPLALIG VYSPELVLPI AETLRVLGYQ RAAVVHSGGM DEVSLHAPTI VAELHDGEIK SYQLTAEDFG LTPYHQDQLA GGTPEENRDI LTRLLQGKGD AAHEAAVAAN VAMLMRLHGQ EDLKANAQTV LDVLRNGTAY DRVTALAARG //