ID   TRPF_BORPE              Reviewed;         218 AA.
AC   Q7VY68;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 94.
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}; OrderedLocusNames=BP1490;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640415; CAE41779.1; -; Genomic_DNA.
DR   RefSeq; NP_880227.1; NC_002929.2.
DR   RefSeq; WP_010930388.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7VY68; -.
DR   SMR; Q7VY68; -.
DR   STRING; 257313.BP1490; -.
DR   PaxDb; 257313-BP1490; -.
DR   GeneID; 69601404; -.
DR   KEGG; bpe:BP1490; -.
DR   PATRIC; fig|257313.5.peg.1598; -.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_076364_2_0_4; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000002676; 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; 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..218
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_1000076432"
SQ   SEQUENCE   218 AA;  22896 MW;  96C49131CB48A870 CRC64;
     MRTRVKICGL TREQDIASAV QAGADAIGFV FYPASKRHVD PARAAQLRRE VPAFVDVVAL
     FVNPRPDEVQ AVLDHVAPDL LQFHGDETPQ DCGRYGRRYL RAFRAGAPGL DSAAGLAAAC
     RQYADAAGWL FDSYSAGYGG SGQGFDHGLL AGVQADPASC AIVLAGGLHP GNVADAVRAV
     RPWAVDVSSG VEDAPGIKSA GKIRQLMAAI KSVDQVAR
//