ID TRPG_SALTY STANDARD; PRT; 530 AA. AC P00905; DT 21-JUL-1986 (Rel. 01, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, 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. OS Salmonella typhimurium. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC 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 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 + PYROPHOSPHATE. CC -!- PATHWAY: FIRST AND SECOND STEPS IN BIOSYNTHESIS OF TRYPTOPHAN. 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: TO OTHER TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAINS. 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; J01811; AAA57312.1; -. DR PIR; A01126; NNEB2T. DR HSSP; Q06129; 1QDL. DR StyGene; SG10399; trpD. DR InterPro; IPR002385; Anth_synthII. DR InterPro; IPR000991; GATase_1. DR InterPro; IPR000312; Glycos_transf_3. 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; PR00096; GATASE. DR ProDom; PD001864; Glycos_transf_3; 1. DR PROSITE; PS00442; GATASE_TYPE_I; 1. KW Tryptophan biosynthesis; Transferase; Lyase; Multifunctional enzyme; KW Glutamine amidotransferase. FT INIT_MET 0 0 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. 2). SQ SEQUENCE 530 AA; 56801 MW; 256D30FE31FD84C7 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 EDLKANAQTL LDVLRNGTAY DRVTALAARG //