TRPC_SALTY
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 03-AUG-2022, entry version 139.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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}.
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DR EMBL; M30286; 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; P00910; -.
DR EnsemblBacteria; AAL20643; AAL20643; STM1725.
DR GeneID; 1253244; -.
DR KEGG; stm:STM1725; -.
DR PATRIC; fig|99287.12.peg.1821; -.
DR HOGENOM; CLU_007713_0_0_6; -.
DR OMA; YDIIGIN; -.
DR PhylomeDB; P00910; -.
DR BioCyc; SENT99287:STM1725-MON; -.
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; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR CDD; cd00331; IGPS; 1.
DR CDD; cd00405; PRAI; 1.
DR Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR22854; PTHR22854; 1.
DR Pfam; PF00218; IGPS; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; SSF51366; 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
