ID TRPF_OCEIH Reviewed; 204 AA. AC Q8ESU3; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 106. 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}; OrderedLocusNames=OB0523; OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / OS KCTC 3954 / HTE831). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus. OX NCBI_TaxID=221109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831; RX PubMed=12235376; DOI=10.1093/nar/gkf526; RA Takami H., Takaki Y., Uchiyama I.; RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge RT and its unexpected adaptive capabilities to extreme environments."; RL Nucleic Acids Res. 30:3927-3935(2002). 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; BA000028; BAC12479.1; -; Genomic_DNA. DR RefSeq; WP_011064926.1; NC_004193.1. DR AlphaFoldDB; Q8ESU3; -. DR SMR; Q8ESU3; -. DR STRING; 221109.gene:10732727; -. DR KEGG; oih:OB0523; -. DR eggNOG; COG0135; Bacteria. DR HOGENOM; CLU_076364_1_0_9; -. DR OrthoDB; 9786954at2; -. DR PhylomeDB; Q8ESU3; -. DR UniPathway; UPA00035; UER00042. DR Proteomes; UP000000822; 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..204 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT /id="PRO_0000154368" SQ SEQUENCE 204 AA; 22232 MW; 3BC4EC004CA20B76 CRC64; MFVKICGITS IDTAQAVVDA NADMIGFVFA PSKRQLSTSL AEEIANTLPQ TIQKVGVFVD EPLENILSII ERVNLDIVQL HGDESIDYQK RIPIPIIKAF PATTEGLNQA NQSSAKYILI DSPPLQSSRG GNGVTFNWNI LKDQPFTSKL ILAGGLNTEN IREAIKTVNP AGVDVSSGVE TNGKKDAKKI QQFITNVQRK DVLR //