ID TRPF_LACP7 Reviewed; 218 AA. AC A9KL42; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 78. 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=Cphy_3844; OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OS (Clostridium phytofermentans). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae. OX NCBI_TaxID=357809; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700394 / DSM 18823 / ISDg; RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E.A., Richardson P.; RT "Complete genome sequence of Clostridium phytofermentans ISDg."; RL Submitted (NOV-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; CP000885; ABX44191.1; -; Genomic_DNA. DR RefSeq; WP_012201839.1; NC_010001.1. DR AlphaFoldDB; A9KL42; -. DR SMR; A9KL42; -. DR STRING; 357809.Cphy_3844; -. DR KEGG; cpy:Cphy_3844; -. DR eggNOG; COG0135; Bacteria. DR HOGENOM; CLU_076364_1_0_9; -. DR OrthoDB; 9786954at2; -. DR UniPathway; UPA00035; UER00042. DR Proteomes; UP000000370; 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_1000197095" SQ SEQUENCE 218 AA; 24895 MW; E02A3D72ACA435CC CRC64; MKTKICGLKS LREIEIVNKY APNYVGFVFA GVKRKIDEEV ASLLRRELSS EIQAVGVFVN ESIERIAKMC EKNTIQLVQL HGDEDRDYIN ALKLEVGAPI IKAVRAQSVE QILEALTLPC DYFLYDTYSE HSYGGEGKRF DETILTEVYK ESSNNEFKKY LQKPYFIAGG LTAQNVRLLD SRLEPYGVDV SSGVESMGQK DEEKVKEFLF AAWRWNEN //