ID   TRPF_PRIM1              Reviewed;         208 AA.
AC   P70938; D5DRF1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE            Short=PRAI;
DE            EC=5.3.1.24;
GN   Name=trpF; OrderedLocusNames=BMQ_4320;
OS   Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=545693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12872 / QMB1551;
RX   PubMed=21705586; DOI=10.1128/jb.00449-11;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA   Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA   Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA   Bremer E., Jahn D., Ravel J., Vary P.S.;
RT   "Genome sequences of the biotechnologically important Bacillus megaterium
RT   strains QM B1551 and DSM319.";
RL   J. Bacteriol. 193:4199-4213(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-113.
RA   Jablonski L.M., Vary P.S., Hudspeth D.S.;
RL   Submitted (SEP-1996) 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; CP001983; ADE71330.1; -; Genomic_DNA.
DR   EMBL; U67986; AAB07593.1; -; Genomic_DNA.
DR   RefSeq; WP_013059003.1; NC_014019.1.
DR   AlphaFoldDB; P70938; -.
DR   SMR; P70938; -.
DR   STRING; 545693.BMQ_4320; -.
DR   EnsemblBacteria; ADE71330; ADE71330; BMQ_4320.
DR   GeneID; 64145974; -.
DR   KEGG; bmq:BMQ_4320; -.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_076364_2_0_9; -.
DR   OMA; FYAKSPR; -.
DR   OrthoDB; 1854712at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000000935; 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..208
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_0000154346"
SQ   SEQUENCE   208 AA;  23399 MW;  3E4EF5CD8A1E869C CRC64;
     MLIKYCGIRS KQDIALIEKS AATHIGFIFY PRSKRYVKPE RVNEFVTDEI KKQVSLVGVF
     VNTPVDQILE IASVTNLDVI QCHGQETAAD VRQLKQRGYE VWKALPHNKE TLQQMHVYEE
     ADGYVIDSKV KEQFGGTGVA FDWSFVPQYE SAAQRLGKKC FIAGGINACN IENLLPYQPG
     AIDISGGIET NGTKDYTKII EIERKIIL