ID   TRPF_THEKO              Reviewed;         208 AA.
AC   Q9YGB1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE            Short=PRAI;
DE            EC=5.3.1.24;
GN   Name=trpF; OrderedLocusNames=TK0256;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=10628865; DOI=10.1007/s004380051145;
RA   Tang X., Ezaki S., Fujiwara S., Takagi M., Atomi H., Imanaka T.;
RT   "The tryptophan biosynthesis gene cluster trpCDEGFBA from Pyrococcus
RT   kodakaraensis KOD1 is regulated at the transcriptional level and expressed
RT   as a single mRNA.";
RL   Mol. Gen. Genet. 262:815-821(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5.
CC   -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000305}.
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DR   EMBL; AB030011; BAA82549.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD84445.1; -; Genomic_DNA.
DR   PIR; T43926; T43926.
DR   RefSeq; WP_011249211.1; NC_006624.1.
DR   PDB; 5LHE; X-ray; 1.85 A; A=2-208.
DR   PDB; 5LHF; X-ray; 1.75 A; A/B=1-208.
DR   PDBsum; 5LHE; -.
DR   PDBsum; 5LHF; -.
DR   AlphaFoldDB; Q9YGB1; -.
DR   SMR; Q9YGB1; -.
DR   STRING; 69014.TK0256; -.
DR   EnsemblBacteria; BAD84445; BAD84445; TK0256.
DR   GeneID; 3235375; -.
DR   KEGG; tko:TK0256; -.
DR   PATRIC; fig|69014.16.peg.255; -.
DR   eggNOG; arCOG01983; Archaea.
DR   HOGENOM; CLU_076364_2_1_2; -.
DR   InParanoid; Q9YGB1; -.
DR   OMA; HDHRISQ; -.
DR   OrthoDB; 117266at2157; -.
DR   PhylomeDB; Q9YGB1; -.
DR   BRENDA; 5.3.1.24; 5246.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Isomerase; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..208
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_0000154413"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   HELIX           13..19
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   TURN            20..22
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   STRAND          24..29
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   HELIX           40..49
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   STRAND          54..58
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   HELIX           63..73
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   HELIX           86..96
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   STRAND          99..105
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   STRAND          110..112
FT                   /evidence="ECO:0007829|PDB:5LHE"
FT   HELIX           113..125
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   STRAND          130..135
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   HELIX           142..155
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   STRAND          159..163
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   TURN            166..168
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   HELIX           169..176
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   STRAND          179..184
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   HELIX           185..187
FT                   /evidence="ECO:0007829|PDB:5LHF"
FT   HELIX           195..206
FT                   /evidence="ECO:0007829|PDB:5LHF"
SQ   SEQUENCE   208 AA;  23049 MW;  54D5DDB85F9312A8 CRC64;
     MVEFVKICGV KTMDELRLVE RYADATGVVV NSRSKRKVPL KTAAELIEMA EIPIYLVSTM
     KTFPEWANAV EKTGAEYIQV HSDMHPKAVN RLKDEYGVSV MKAFMVPRES DDPAEDAERL
     LELIGQYEVD KILLDTGVGS GRRHDYRVSA IIAKEYPIVL AGGLTPENVG EAIRWVKPAG
     VDVSSGVERN GVKDRVLIEA FMAVVRNG