ID   TRPF_CERS4              Reviewed;         212 AA.
AC   Q9X4E3; Q3IW94;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE            Short=PRAI;
DE            EC=5.3.1.24;
GN   Name=trpF; OrderedLocusNames=RHOS4_36220; ORFNames=RSP_3587;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10511537; DOI=10.1093/genetics/153.2.525;
RA   Mackenzie C., Simmons A.E., Kaplan S.;
RT   "Multiple chromosomes in bacteria. The yin and yang of trp gene
RT   localization in Rhodobacter sphaeroides 2.4.1.";
RL   Genetics 153:525-538(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-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;
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; AF107093; AAD29259.1; -; Genomic_DNA.
DR   EMBL; CP000144; ABA81190.1; -; Genomic_DNA.
DR   RefSeq; WP_011339435.1; NZ_CP030272.1.
DR   RefSeq; YP_355091.1; NC_007494.2.
DR   AlphaFoldDB; Q9X4E3; -.
DR   SMR; Q9X4E3; -.
DR   STRING; 272943.RSP_3587; -.
DR   EnsemblBacteria; ABA81190; ABA81190; RSP_3587.
DR   KEGG; rsp:RSP_3587; -.
DR   PATRIC; fig|272943.9.peg.4023; -.
DR   eggNOG; COG0135; Bacteria.
DR   OMA; FYAKSPR; -.
DR   PhylomeDB; Q9X4E3; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000002703; Chromosome 2.
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..212
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_0000154375"
SQ   SEQUENCE   212 AA;  22142 MW;  DF2D9294D0D8ACAC CRC64;
     MAGVRVKICG LRTESDVKAA ASSGAAYVGL VFFPKSPRHL ELAQAQRLAL AAPPGVAKVA
     LTVDASDETL DAIVEAVPLD MLQLHGGESP ERVAEVRARY GLPVMKAVGV ADEGDLPQIL
     EQSLAADQIL IDAKPPKGAA LPGGNGLSFD WRLISGRHWI RPWMLAGGLT VENLAEAVRR
     TGASQVDVSS GVESAPGVKD PARIAAFLQA AR