ID   TRPF_ERYLH              Reviewed;         209 AA.
AC   Q2N9N2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=ELI_07585;
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=314225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2594;
RX   PubMed=19168610; DOI=10.1128/jb.00026-09;
RA   Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL   J. Bacteriol. 191:2419-2420(2009).
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}.
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; CP000157; ABC63609.1; -; Genomic_DNA.
DR   RefSeq; WP_011414443.1; NC_007722.1.
DR   AlphaFoldDB; Q2N9N2; -.
DR   SMR; Q2N9N2; -.
DR   STRING; 314225.ELI_07585; -.
DR   EnsemblBacteria; ABC63609; ABC63609; ELI_07585.
DR   KEGG; eli:ELI_07585; -.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_076364_1_1_5; -.
DR   OMA; FYAKSPR; -.
DR   OrthoDB; 1854712at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000008808; 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..209
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_1000018594"
SQ   SEQUENCE   209 AA;  22364 MW;  76122A1A646B25AB CRC64;
     MTMIKICGLS TPETIEAAVQ AGATHVGLVH FAKSPRHVEL EKAAELRALV PESVKAVLLL
     VNEQPEETAR AIQIVKPDVV QFHGSETPQW TKAVRDQLGI EVWKALGVRE AATLEKSRRY
     EGAVDRLLFD SPAKKLPGGN GVTFQWDVLA GFEHHTAWGL AGGLTPDNVG DAIRQTGAEL
     VDASSGVESA PGVKDIAKIE AFCEAARNA