TRPC_ECO57
ID TRPC_ECO57 Reviewed; 453 AA.
AC Q8X7B7;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 3.
DT 03-AUG-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=Z2549, ECs1834;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(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. {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; AE005174; AAG56554.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35257.1; -; Genomic_DNA.
DR PIR; B90858; B90858.
DR PIR; F85761; F85761.
DR RefSeq; NP_309861.1; NC_002695.1.
DR RefSeq; WP_000983857.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X7B7; -.
DR SMR; Q8X7B7; -.
DR STRING; 155864.EDL933_2429; -.
DR EnsemblBacteria; AAG56554; AAG56554; Z2549.
DR EnsemblBacteria; BAB35257; BAB35257; ECs_1834.
DR GeneID; 912854; -.
DR KEGG; ece:Z2549; -.
DR KEGG; ecs:ECs_1834; -.
DR PATRIC; fig|386585.9.peg.1933; -.
DR eggNOG; COG0134; Bacteria.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_007713_0_0_6; -.
DR UniPathway; UPA00035; UER00042.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..453
FT /note="Tryptophan biosynthesis protein TrpCF"
FT /id="PRO_0000154278"
FT REGION 1..257
FT /note="Indole-3-glycerol phosphate synthase"
FT REGION 258..453
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
SQ SEQUENCE 453 AA; 49433 MW; 7C30E71A58270033 CRC64;
MMQTVLAKIV ADKAIWVEAR KQQQPLASFQ NEVQPSTRHF YDALQGARTA FILECKKASP
SKGVICDDFD PARIAAIYKH YASAISVLTD EKYFQGSFDF LPIVSQIAPQ PILCKDFIID
PYQIYLARYY QADACLLMLS VLDDEQYRQL AAVAHSLKMG VLTEVSNEEE LERAIALGAK
VVGINNRDLR DLSIDLNRTR ELAPKLGHNV TVISESGINT YAQVRELSHF ADGFLIGSAL
MAHDDLHAAV RRVLLGENKV CGLTRGQDAK AAYDAGAIYG GLIFVATSPR CVNVEQAQEV
MAAAPLQYVG VFRNHDIADV LDKAKVLSLV AVQLHGNEDQ LYIDTLREAL PAHVAIWKAL
SVGETLPARE LQHVDKYVLD NGQGGSGQRF DWSLLNGQSL GNVLLAGGLG ADNCVEAAQT
GCAGLDFNSA VESQPGIKDA RLLASVFQTL RAY
