ID TRPF_METM7 Reviewed; 208 AA. AC A6VFU0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 71. 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=MmarC7_0246; OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=426368; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C7 / ATCC BAA-1331; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.; RT "Complete sequence of Methanococcus maripaludis C7."; RL Submitted (JUN-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; CP000745; ABR65316.1; -; Genomic_DNA. DR AlphaFoldDB; A6VFU0; -. DR SMR; A6VFU0; -. DR STRING; 426368.MmarC7_0246; -. DR KEGG; mmz:MmarC7_0246; -. DR eggNOG; arCOG01983; Archaea. DR HOGENOM; CLU_076364_2_1_2; -. DR OrthoDB; 27513at2157; -. 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..208 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT /id="PRO_1000057878" SQ SEQUENCE 208 AA; 23247 MW; C5E34FF21C7A0926 CRC64; MFIKICGIKT PEELEIVESY GNATGVILEC ASKRRIGLET AKNLVNLSNI PVFAVSTTSE VLVWENIIKL TNTNYLQMHS DIDQKTIDFI KNEYGCFIMK SFKIPETSES PEIDAEKIIS DIETYEVDRI LLDTGKGCGQ THDHRISQII AKKFDIILAG GLDPDNVFDI VKNVKPFGVD VSSGVEANNS KDEELIKRFC ENVKSVKL //