ID TRPF_ALCBS Reviewed; 218 AA. AC Q0VPI8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 23. DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase; DE Short=PRAI; DE EC=5.3.1.24; GN Name=trpF; OrderedLocusNames=ABO_1462; OS Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., RA Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., RA Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., RA Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A., RA Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., RA Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine RT bacterium Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(2006). CC -!- CATALYTIC ACTIVITY: N-(5-phospho-beta-D-ribosyl)anthranilate = 1- CC (2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. CC -!- SIMILARITY: Belongs to the trpF family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM286690; CAL16910.1; -; Genomic_DNA. DR RefSeq; YP_693182.1; -. DR GeneID; 4211821; -. DR GenomeReviews; AM286690_GR; ABO_1462. DR KEGG; abo:ABO_1462; -. DR NMPDR; fig|393595.12.peg.1468; -. DR HOGENOM; Q0VPI8; -. DR OMA; Q0VPI8; PVIRAIQ. DR BioCyc; ABOR393595:ABO_1462-MON; -. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:HAMAP. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00135; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001240; PRAI. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Pfam; PF00697; PRAI; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Isomerase; Tryptophan biosynthesis. FT CHAIN 1 218 N-(5'-phosphoribosyl)anthranilate FT isomerase. FT /FTId=PRO_1000018575. SQ SEQUENCE 218 AA; 22908 MW; DC0D0E5C2BE36734 CRC64; MTVPRVKICG ITRIEDGLAA ANAGADAIGL VFYGPSPRAV TARQAAEICA SLPPFVTTVA LFVDASRAEI EGVLARVPVD LLQFHGNENP QFCDSFNRPW IKAVRMKDDV DLHHYAQIYR NAAGLLIDSY VAGVPGGTGE TFNWGRVPKT LPLPVVLAGG LHPGNVAAAV TQVQPWAVDV SGGVEQKNVQ GGRSGGIKDA SAIRVFINSV KTRGVAGV //