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 10-MAY-2005 (Rel. 47, 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 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. 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 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 OF 1-200. 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: 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. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 2. 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 -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate CC phosphoribosyltransferase family. CC -!- SIMILARITY: Contains 1 type-1 glutamine amidotransferase 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 PDB; 1I1Q; X-ray; B=1-192. DR SMR; P00905; 198-529. DR StyGene; SG10399; trpD. DR HAMAP; MF_00211; fused; 1. DR InterPro; IPR005940; Ant_phspho_trans. DR InterPro; IPR006220; Anth_synthII. DR InterPro; IPR001317; CP_synthGATase. DR InterPro; IPR011702; GATASE. DR InterPro; IPR000991; GATase_1. DR InterPro; IPR012998; GATASE_TYPE1_AS. DR InterPro; IPR000312; Glyco_trans_3. DR InterPro; IPR006221; TrpG_papA. 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; PS00442; GATASE_TYPE_I; 1. 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 0 0 By similarity. FT REGION 1 200 Glutamine amidotransferase. FT REGION 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). FT STRAND 2 7 FT HELIX 13 22 FT TURN 23 24 FT STRAND 26 31 FT TURN 32 33 FT HELIX 37 43 FT TURN 44 45 FT STRAND 49 53 FT HELIX 60 62 FT TURN 64 65 FT HELIX 66 73 FT STRAND 74 74 FT TURN 75 76 FT STRAND 77 77 FT STRAND 79 82 FT TURN 83 83 FT HELIX 84 92 FT TURN 93 93 FT STRAND 107 113 FT HELIX 117 119 FT TURN 120 121 FT STRAND 126 130 FT TURN 141 142 FT STRAND 144 149 FT TURN 150 151 FT STRAND 152 158 FT TURN 159 162 FT STRAND 163 166 FT STRAND 169 169 FT TURN 170 171 FT TURN 173 174 FT TURN 176 177 FT HELIX 178 189 FT TURN 190 190 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 //