ID   TRPF_BRUME              Reviewed;         222 AA.
AC   P67003; Q8FXY3; Q8YE61;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=BMEI2017;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL53198.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008917; AAL53198.1; ALT_INIT; Genomic_DNA.
DR   PIR; AC3504; AC3504.
DR   RefSeq; WP_002965175.1; NZ_GG703778.1.
DR   AlphaFoldDB; P67003; -.
DR   SMR; P67003; -.
DR   STRING; 224914.BMEI2017; -.
DR   EnsemblBacteria; AAL53198; AAL53198; BMEI2017.
DR   GeneID; 45053036; -.
DR   GeneID; 55591677; -.
DR   KEGG; bme:BMEI2017; -.
DR   PATRIC; fig|224914.52.peg.1553; -.
DR   eggNOG; COG0135; Bacteria.
DR   OMA; FYAKSPR; -.
DR   PhylomeDB; P67003; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000000419; Chromosome I.
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   Tryptophan biosynthesis.
FT   CHAIN           1..222
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_0000154348"
SQ   SEQUENCE   222 AA;  23614 MW;  28E7AFA3258F5514 CRC64;
     MALDIKICGL KTPEAVAAAL DGGATHIGFI FFPKSPRHIT PDAAARLRAA ATGRAVAVAV
     TVDADDEALD EIVKTVRPDM LQLHGGETPE RVRFLKERYN LPVMKAFSIR EAGDLEAIAP
     YRGIADRFLF DAKPPKGSEL PGGNGISFDW NLLAALDADI DYMLSGGLNA DNIAEALLKT
     GAPGIDISSG VECAPGEKDV RLIENFFQAV ADANAQPFAR RA