ID TRPC_SALTY Reviewed; 452 AA. AC P00910; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 28-JAN-2026, entry version 152. DE RecName: Full=Tryptophan biosynthesis protein TrpCF; DE Includes: DE RecName: Full=Indole-3-glycerol phosphate synthase; DE Short=IGPS; DE EC=4.1.1.48; DE Includes: DE RecName: Full=N-(5'-phospho-ribosyl)anthranilate isomerase; DE Short=PRAI; DE EC=5.3.1.24; GN Name=trpC; OrderedLocusNames=STM1725; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX 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 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., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). CC -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of CC tryptophan biosynthetic pathway. The first reaction is catalyzed by the CC isomerase, coded by the TrpF domain; the second reaction is catalyzed CC by the synthase, coded by the TrpC domain (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2- CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; CC EC=5.3.1.24; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) CC = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O; CC Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 4/5. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: In the N-terminal section; belongs to the TrpC family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the TrpF family. CC {ECO:0000305}. 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; AH000942; AAA27237.1; -; Genomic_DNA. DR EMBL; AE006468; AAL20643.1; -; Genomic_DNA. DR PIR; A01132; GWEBT. DR RefSeq; NP_460684.1; NC_003197.2. DR RefSeq; WP_001195296.1; NC_003197.2. DR AlphaFoldDB; P00910; -. DR SMR; P00910; -. DR STRING; 99287.STM1725; -. DR PaxDb; 99287-STM1725; -. DR GeneID; 1253244; -. DR KEGG; stm:STM1725; -. DR PATRIC; fig|99287.12.peg.1821; -. DR HOGENOM; CLU_007713_0_0_6; -. DR OMA; NVKTPFM; -. DR PhylomeDB; P00910; -. DR BioCyc; SENT99287:STM1725-MONOMER; -. DR UniPathway; UPA00035; UER00042. DR UniPathway; UPA00035; UER00043. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000162; P:L-tryptophan biosynthetic process; IBA:GO_Central. DR CDD; cd00331; IGPS; 1. DR CDD; cd00405; PRAI; 1. DR FunFam; 3.20.20.70:FF:000024; Indole-3-glycerol phosphate synthase; 1. DR FunFam; 3.20.20.70:FF:000165; Multifunctional fusion protein; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 2. DR HAMAP; MF_00134_B; IGPS_B; 1. DR HAMAP; MF_00135; PRAI; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR045186; Indole-3-glycerol_P_synth. DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom. DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS. DR InterPro; IPR001240; PRAI_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR NCBIfam; NF001377; PRK00278.2-4; 1. DR NCBIfam; NF006945; PRK09427.1; 1. DR PANTHER; PTHR22854:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1. DR Pfam; PF00218; IGPS; 1. DR Pfam; PF00697; PRAI; 1. DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2. DR PROSITE; PS00614; IGPS; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase; KW Isomerase; Lyase; Multifunctional enzyme; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1..452 FT /note="Tryptophan biosynthesis protein TrpCF" FT /id="PRO_0000154284" FT REGION 1..256 FT /note="Indole-3-glycerol phosphate synthase" FT REGION 257..452 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" SQ SEQUENCE 452 AA; 49202 MW; AF0DC781A2F75859 CRC64; MQTVLAKIVA DKAIWVEARK QQQPLASFQN EIQPSTRHFY DALQGARTAF ILECKKASPS KGVIRDDFDP ARIASIYQHY ASAISVLTDE KYFQGSFDFL PVVSQSAPQP ILCKDFIIDP YQIYLARYYQ ADACLLMLSV LDDEQYRQLS AVAHSLKMGV LTEVSNDEER ERAIALGAKV VGINNRDLRD LSIDLNRTRQ LAPKLGHGVT VISESGINTY GQVRELSHFA NGFLIGSALM AHDDLNAAVR RVLLGENKVC GLTRAQDAKA ACDAGAIYGG LIFVPSSPRA VSVEQAREVI SGAPLQYVGV FKNADIADVC QKAAVLSLSA VQLHGSEDQA YVNALREALP KQVQIWKALS VSDALPARDY HHVDKYIFDN GQGGSGQRFD WSLLQGQPLD NVLLAGGLAA DNCVQAAQVG CAGLDFNSGV ESQPGIKDAR LLASVFQTLR AY //