ID   TRPF_THEYD              Reviewed;         217 AA.
AC   B5YKL4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
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=THEYE_A0943;
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC   Bacteria; Nitrospirota; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC   Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX   NCBI_TaxID=289376;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT   ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) 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; CP001147; ACI21048.1; -; Genomic_DNA.
DR   RefSeq; WP_012545776.1; NC_011296.1.
DR   RefSeq; YP_002248779.1; NC_011296.1.
DR   AlphaFoldDB; B5YKL4; -.
DR   SMR; B5YKL4; -.
DR   STRING; 289376.THEYE_A0943; -.
DR   EnsemblBacteria; ACI21048; ACI21048; THEYE_A0943.
DR   KEGG; tye:THEYE_A0943; -.
DR   PATRIC; fig|289376.4.peg.929; -.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_076364_2_0_0; -.
DR   InParanoid; B5YKL4; -.
DR   OrthoDB; 9786954at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000000718; 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; Aldolase class I; 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; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; 1.
DR   PANTHER; PTHR42894:SF1; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; 1.
DR   Pfam; PF00697; PRAI; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Isomerase;
KW   Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..217
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_1000095948"
SQ   SEQUENCE   217 AA;  24338 MW;  BF4BCAEE76A5A0DA CRC64;
     MIRVKICGIT NIDDALWATE CGADALGFIF YKKSQRYIDP QKAKEIIKAL PPFVNLVGVF
     VNETVENIKE IMAITGIDTV QLHGDETSEF CLNFRKVIKA FRVDNRGYLP NGKSLKDILP
     KYKVSAFLLD SFSENEYGGT GKTFNWDVAL KAKEYGTIIL SGGLNVFNID EAIKKVFPYA
     VDVSSGVELY KGKKDPELVK KFIEKAKLKK IKGEHDD
//