TRPC_SALTI
ID TRPC_SALTI Reviewed; 452 AA.
AC Q8Z7D9;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=STY1326, t1637;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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. {ECO:0000250}.
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; AL513382; CAD08407.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO69264.1; -; Genomic_DNA.
DR RefSeq; NP_455773.1; NC_003198.1.
DR RefSeq; WP_001195287.1; NZ_QWLP01000020.1.
DR AlphaFoldDB; Q8Z7D9; -.
DR SMR; Q8Z7D9; -.
DR STRING; 220341.16502450; -.
DR EnsemblBacteria; AAO69264; AAO69264; t1637.
DR KEGG; stt:t1637; -.
DR KEGG; sty:STY1326; -.
DR PATRIC; fig|220341.7.peg.1333; -.
DR eggNOG; COG0134; Bacteria.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_007713_0_0_6; -.
DR OMA; YDIIGIN; -.
DR UniPathway; UPA00035; UER00042.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
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; Tryptophan biosynthesis.
FT CHAIN 1..452
FT /note="Tryptophan biosynthesis protein TrpCF"
FT /id="PRO_0000154283"
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; 49230 MW; E602F9F59D1DA70E CRC64;
MQTVLAKIVA DKAIWVEARK QQQPLASFQN EIQPSTRHFY DALQGARTAF ILECKKASPS
KGVIRDDFDP ARIASIYQHY ASAISVLTDE KYFQGSFDFL PVVSQSAPQP ILCKDFIIDP
YQIYLARYYQ ADACLLMLSV LDDEQYRQLS AVAHSLKMGV LTEISNDEER ERAIALGAKV
VGINNRDLRD LSIDLNRTRQ LAPKLGHGVT VISESGINTY GQVRELSHFA NGFLIGSALM
AHDDLNAAVR RVLLGENKVC GLTRAQDAKA ACDAGAIYGG LIFVPSSPRA VSVEQAREVI
SGAPLQYVGV FKNADIADVC QKAAVLSLSA VQLHGSEDQA YVNALREALP RNVQIWKALS
VSNALPARDY HHVDKYIFDN GQGGSGQRFD WSLLQGQPLD DVLLAGGLAA DNCVQAAQVG
CAGLDFNSGV ESQPGIKDAR LLASVFQTLR AY
