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 31-OCT-2012, entry version 124. DE RecName: Full=Anthranilate synthase component II; DE EC=4.1.3.27; DE Includes: DE RecName: Full=Glutamine amidotransferase; DE Includes: DE RecName: Full=Anthranilate phosphoribosyltransferase; DE EC=2.4.2.18; GN Name=trpD; Synonyms=trpGD; OrderedLocusNames=STM1724; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; 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 -!- 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; AE006468; AAL20642.1; -; Genomic_DNA. DR EMBL; J01811; AAA57312.1; -; Genomic_DNA. DR PIR; A92907; NNEB2T. DR RefSeq; NP_460683.1; NC_003197.1. DR PDB; 1I1Q; X-ray; 1.90 A; B=2-192. DR PDBsum; 1I1Q; -. DR ProteinModelPortal; P00905; -. DR SMR; P00905; 2-193, 199-530. DR IntAct; P00905; 1. DR MINT; MINT-189132; -. DR PRIDE; P00905; -. DR GeneID; 1253243; -. DR GenomeReviews; AE006468_GR; STM1724. DR KEGG; stm:STM1724; -. DR PATRIC; 32381961; VBISalEnt20916_1820. DR eggNOG; COG0547; -. DR HOGENOM; HOG000230451; -. DR KO; K13497; -. DR OMA; NAMFALY; -. DR ProtClustDB; PRK09522; -. DR BioCyc; STYP99287:STM1724-MONOMER; -. DR UniPathway; UPA00035; UER00040. DR UniPathway; UPA00035; UER00041. DR EvolutionaryTrace; P00905; -. DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:EC. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:EC. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; G3DSA:3.40.1030.10; Glyco_trans_3; 2. DR HAMAP; MF_00211; TrpD; 1; fused. DR InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase. DR InterPro; IPR017926; GATASE_1. DR InterPro; IPR000312; Glycosyl_Trfase_fam3. DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom. 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 SUPFAM; SSF47648; Glyco_trans_3; 1. DR SUPFAM; SSF52418; 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; Reference proteome; Transferase; KW 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 3 8 FT HELIX 14 23 FT STRAND 27 32 FT HELIX 38 44 FT STRAND 48 54 FT HELIX 61 63 FT HELIX 67 74 FT STRAND 80 83 FT HELIX 85 93 FT STRAND 106 114 FT HELIX 118 120 FT STRAND 125 131 FT STRAND 145 150 FT STRAND 153 159 FT TURN 160 163 FT STRAND 164 170 FT HELIX 179 190 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 //