ID   TRPF_SYNE7              Reviewed;         217 AA.
AC   Q31R79;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
GN   OrderedLocusNames=Synpcc7942_0408;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000100; ABB56440.1; -; Genomic_DNA.
DR   RefSeq; WP_011377568.1; NC_007604.1.
DR   AlphaFoldDB; Q31R79; -.
DR   SMR; Q31R79; -.
DR   STRING; 1140.Synpcc7942_0408; -.
DR   PRIDE; Q31R79; -.
DR   EnsemblBacteria; ABB56440; ABB56440; Synpcc7942_0408.
DR   KEGG; syf:Synpcc7942_0408; -.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_076364_2_0_3; -.
DR   OMA; FYAKSPR; -.
DR   OrthoDB; 1854712at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_0408-MON; -.
DR   UniPathway; UPA00035; UER00042.
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   Tryptophan biosynthesis.
FT   CHAIN           1..217
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_1000197132"
SQ   SEQUENCE   217 AA;  23299 MW;  F7879C5153CC129E CRC64;
     MGLRIKICGL RDPQQAIAIA DLGATAIGFI AVRQSPRYVS PAQVAEIAQA LQKTHPTVNR
     VGVFANATAE ELEAYVAAGI TSLQLHGDET LADCQRWRDR FPALELIKAL RIRSTADLAL
     AESFTDCVDT LLLDAYHPQM LGGTGATLDW QALQAFQPSR PWLLAGGLTP ENITTALSQL
     HPAGIDLSSG VERSPGDKDL EKVTALFSSL ARNSLLK