ID   TRPF_THENN              Reviewed;         205 AA.
AC   B9K6Z3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=CTN_0550;
OS   Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=309803;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA   Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA   Kim J.J., Park K.J., Lee S.Y.;
RT   "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT   neapolitana.";
RL   Submitted (NOV-2007) 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; CP000916; ACM22726.1; -; Genomic_DNA.
DR   RefSeq; WP_015919045.1; NC_011978.1.
DR   AlphaFoldDB; B9K6Z3; -.
DR   SMR; B9K6Z3; -.
DR   STRING; 309803.CTN_0550; -.
DR   EnsemblBacteria; ACM22726; ACM22726; CTN_0550.
DR   KEGG; tna:CTN_0550; -.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_076364_2_0_0; -.
DR   OMA; FYAKSPR; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000000445; 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   Tryptophan biosynthesis.
FT   CHAIN           1..205
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_1000197134"
SQ   SEQUENCE   205 AA;  22914 MW;  C818FF3BE5F80799 CRC64;
     MVRVKICGIT NLEDALFSVE SGADAVGFVF YSKSKRYVSP EKAREISLNL PPFVFRVGVF
     VNESLESVLD IAFHAGLNAV QLHGDESVEF CERLNEKIMV IKAVGISEEQ DVRRALEYRK
     FPVLLDTKVS GYGGSGKVFN WSVVLPYRDQ FRYLILSGGL NPRNVERAIE MVRPFAVDVS
     SGVEISPGKK DHNLVREFIK KAKGL