ID TRPF_CHLPM Reviewed; 217 AA. AC A4SF78; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 27-MAR-2024, 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}; GN OrderedLocusNames=Cvib_1123; OS Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris OS vibrioformis (strain DSM 265)). OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290318; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 265 / 1930; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., RA Schuster S.C., Bryant D.A., Richardson P.; RT "Complete sequence of Prosthecochloris vibrioformis DSM 265."; RL Submitted (MAR-2007) 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; CP000607; ABP37137.1; -; Genomic_DNA. DR AlphaFoldDB; A4SF78; -. DR SMR; A4SF78; -. DR STRING; 290318.Cvib_1123; -. DR KEGG; pvi:Cvib_1123; -. DR eggNOG; COG0135; Bacteria. DR HOGENOM; CLU_076364_2_0_10; -. DR OrthoDB; 9786954at2; -. 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..217 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT /id="PRO_1000197115" SQ SEQUENCE 217 AA; 23466 MW; 1842C556AE71A31F CRC64; MTRTKICGIT RLNDALHASS EGVDALGFNF SRKSPRSITP SAAKKIIDEL PPFVSKVGIF VEQSPAEIAD ICSYSKIAVA QLHSERYSAA DARFLKDMVH VIRVFRPDGS FSPQSLTPFA EESGVRTFLF DAYKEGMEGG TGEEIETSVA RQIFPAEGAP FFRVLAGGLN PGNVAEAIRQ FRPYGVDTAS GVEAKPGIKD PEKISAFLLA VRLANQP //