ID   TRPF_LACLA              Reviewed;         351 AA.
AC   Q02002;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE            Short=PRAI;
DE            EC=5.3.1.24;
GN   Name=trpF; OrderedLocusNames=LL1466; ORFNames=L0050;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=1400208; DOI=10.1128/jb.174.20.6563-6570.1992;
RA   Bardowski J., Ehrlich S.D., Chopin A.;
RT   "Tryptophan biosynthesis genes in Lactococcus lactis subsp. lactis.";
RL   J. Bacteriol. 174:6563-6570(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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: In the N-terminal section; belongs to the TrpF family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: To B.subtilis YnaI in the C-terminal section.
CC       {ECO:0000305}.
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DR   EMBL; M87483; AAA25227.1; -; Genomic_DNA.
DR   EMBL; AE005176; AAK05564.1; -; Genomic_DNA.
DR   PIR; S35128; S35128.
DR   RefSeq; NP_267622.1; NC_002662.1.
DR   RefSeq; WP_003130430.1; NC_002662.1.
DR   AlphaFoldDB; Q02002; -.
DR   SMR; Q02002; -.
DR   STRING; 272623.L0050; -.
DR   PaxDb; Q02002; -.
DR   EnsemblBacteria; AAK05564; AAK05564; L0050.
DR   KEGG; lla:L0050; -.
DR   PATRIC; fig|272623.7.peg.1576; -.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_787062_0_0_9; -.
DR   OMA; DWDSINP; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000002196; 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   Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..351
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_0000154359"
FT   REGION          1..198
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
SQ   SEQUENCE   351 AA;  39586 MW;  698A3934C9EFD89F CRC64;
     MKIKICGLST KEAVDTAVES GVTHLGFILS PSKRQVAPEK ILQITNDVPK TVKKVGVFVD
     EPIDFVKKAI QVAQLDLVQL HGNEDMNYIN QLDISVIKAI RPDQEFKEYE DVILLFDSPQ
     AGSGQAFDWD SLVTSGLKNK FFIAGGLNPE NVAAAIQHFP NAYGVDVSSG VETDGIKNLT
     KIKNFVQNAS LASSKQLFIE FLRITKKLNE NKIIPYLMGS LAVEQIINFP TNPDDIDIQL
     KTSDFENFEQ LTSLMEKLGY QLIDLHEHKF EKASIHVGFA SVETLKNYAG VDYLTIQQER
     MENGEKYHLP NVEQSLKIYE AAKRDEWRGG KQKDSFIFDE LIKEQKRNDN E