ID TRPF_BACAA Reviewed; 204 AA. AC C3P3T9; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 27-MAR-2024, entry version 61. 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}; GN OrderedLocusNames=BAA_1328; OS Bacillus anthracis (strain A0248). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=592021; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A0248; RA Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D., RA Brettin T.; RT "Genome sequence of Bacillus anthracis A0248."; RL Submitted (APR-2009) 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; 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001598; ACQ50330.1; -; Genomic_DNA. DR RefSeq; WP_000865112.1; NC_012659.1. DR AlphaFoldDB; C3P3T9; -. DR SMR; C3P3T9; -. DR GeneID; 45021252; -. DR KEGG; bai:BAA_1328; -. DR HOGENOM; CLU_076364_1_0_9; -. DR UniPathway; UPA00035; UER00042. 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 Tryptophan biosynthesis. FT CHAIN 1..204 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT /id="PRO_1000197073" SQ SEQUENCE 204 AA; 22619 MW; F153422997A4D765 CRC64; MKVKICGITD METAKRACEY GADALGFVFA ESKRKITPGL AKEIIQELPA NVLKIGVFVN ESVEVIQKIT GNCGLTHVQL HGGEDNHQIR RLNIPSIKSL GVTSESDMKN AQGYETDYIL FDSPKEKFHG GNGKTFPWEL LAHMPKELRE KTILAGGLNT LNIEEAIRTV RPYMVDVSSG VETEGKKDVE KIKQFIIKAK ECSK //