ID   TRPF_CHLTR              Reviewed;         208 AA.
AC   O84331;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE            Short=PRAI;
DE            EC=5.3.1.24;
GN   Name=trpF; OrderedLocusNames=CT_327;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC67920.1; -; Genomic_DNA.
DR   PIR; D71529; D71529.
DR   RefSeq; NP_219834.1; NC_000117.1.
DR   RefSeq; WP_009871676.1; NC_000117.1.
DR   AlphaFoldDB; O84331; -.
DR   SMR; O84331; -.
DR   STRING; 272561.CT_327; -.
DR   EnsemblBacteria; AAC67920; AAC67920; CT_327.
DR   GeneID; 884791; -.
DR   KEGG; ctr:CT_327; -.
DR   PATRIC; fig|272561.5.peg.352; -.
DR   HOGENOM; CLU_076364_1_0_0; -.
DR   InParanoid; O84331; -.
DR   OrthoDB; 9786954at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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..208
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_0000154355"
SQ   SEQUENCE   208 AA;  22739 MW;  586B86A93AEF705C CRC64;
     MKVKICGITH PDDAREAAKA GADYIGMIFA KDSRRCVSEE KAKYIVEAIQ EGNSEPVGVF
     PEHSVEEILA ITETTGITSI QLSGEDILFK FSQLREHFSI FYVVSVYSNG QPSAALPPMN
     DAVTVVYDHI GGERGSPFDW KAFSPFQHNN WMLGGGVNLW NIKEGISLLS PRGIDVSSGV
     ECPGILRKDI FLMQALINSA KELSSSTL
//