ID   TRPF_PARD8              Reviewed;         221 AA.
AC   A6L9J9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000255|HAMAP-Rule:MF_00135};
DE            Short=PRAI {ECO:0000255|HAMAP-Rule:MF_00135};
DE            EC=5.3.1.24 {ECO:0000255|HAMAP-Rule:MF_00135};
GN   Name=trpF {ECO:0000255|HAMAP-Rule:MF_00135}; OrderedLocusNames=BDI_0587;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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:0000255|HAMAP-Rule:MF_00135};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00135}.
CC   -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00135}.
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DR   EMBL; CP000140; ABR42363.1; -; Genomic_DNA.
DR   RefSeq; WP_011966082.1; NC_009615.1.
DR   AlphaFoldDB; A6L9J9; -.
DR   SMR; A6L9J9; -.
DR   STRING; 435591.BDI_0587; -.
DR   EnsemblBacteria; ABR42363; ABR42363; BDI_0587.
DR   KEGG; pdi:BDI_0587; -.
DR   PATRIC; fig|435591.13.peg.572; -.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_076364_1_2_10; -.
DR   OMA; FYAKSPR; -.
DR   OrthoDB; 1854712at2; -.
DR   BioCyc; PDIS435591:G1G5A-604-MON; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000000566; Chromosome.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00405; PRAI; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00135; PRAI; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001240; PRAI_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR044643; TrpF_fam.
DR   PANTHER; PTHR42894; PTHR42894; 1.
DR   Pfam; PF00697; PRAI; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Isomerase;
KW   Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..221
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_1000197114"
SQ   SEQUENCE   221 AA;  25196 MW;  6E827F414F789995 CRC64;
     MIIKVCGMRE PQNIREVAAL AINWIGFIFY ERSKRFVERC PTEQQATDSE QLSPKKVGVF
     VNATIESMME KASTYKLDYL QLHGNESPED CHTLQKRGYS LIKAFPIATK EDFEKTREYE
     GRVDYFLFDT RCEGYGGSGK RFDWSILTGY KGETPFLLSG GIRPENAEAI RNFRHPRFAG
     IDLNSGFEIE PGLKDIDKLK NFIQQILHPA VETGRAPSPT V