ID Q9EVB9_ECOLX Unreviewed; 300 AA.
AC Q9EVB9;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|ARBA:ARBA00022272};
DE EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362};
DE EC=5.3.1.24 {ECO:0000256|ARBA:ARBA00012572};
DE Flags: Fragment;
GN Name=trpC {ECO:0000313|EMBL:AAG14869.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:AAG14869.1};
RN [1] {ECO:0000313|EMBL:AAG14869.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10954745; DOI=10.1073/pnas.180094797;
RA Pupo G.M., Lan R., Reeves P.R.;
RT "Multiple independent origins of Shigella clones of Escherichia coli and
RT convergent evolution of many of their characteristics.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10567-10572(2000).
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 Evidence={ECO:0000256|ARBA:ARBA00001633};
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; Evidence={ECO:0000256|ARBA:ARBA00001164};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696}.
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; AF293312; AAG14869.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9EVB9; -.
DR UniPathway; UPA00035; UER00042.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00405; PRAI; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR HAMAP; MF_00135; PRAI; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR InterPro; IPR001240; PRAI_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR044643; TrpF_fam.
DR PANTHER; PTHR42894; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; 1.
DR PANTHER; PTHR42894:SF1; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; 1.
DR Pfam; PF00218; IGPS; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:AAG14869.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}.
FT DOMAIN 1..99
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 105..295
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAG14869.1"
SQ SEQUENCE 300 AA; 32203 MW; 227F086C2D4D1956 CRC64;
AHSLEMGVLT EVSNEEELER AIALGAKVVG INNRDLRDLS IDLNRTRELA PKLGHNVTVI
SESGINTYAQ VRELSHFANG FLIGSALMAH DDLHAAVRRV LLGENKVCGL TRGQDAKAAY
DAGAIYGGLI FVATSPRCVN VEQAQEVMAA APLQYVGVFR NHDIADVVDK AKVLSLAAVQ
LHSNEDQLYI DTLREALPAH VAIWKALSVG ETLPTREFQH VDKYVLDNGQ GGSGQRFDWS
LLNGQSLGNV LLAGGLGADN CVEAAQTGCA GLDFNSAVES QPGIKDARLL ASFFQTLRAY
//
