ID TRPF_GEOSL Reviewed; 203 AA. AC Q74AH7; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 99. 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=GSU2378; OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA). OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=243231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51573 / DSM 12127 / PCA; RX PubMed=14671304; DOI=10.1126/science.1088727; RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C., RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J., RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A., RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E., RA Lovley D.R., Fraser C.M.; RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface RT environments."; RL Science 302:1967-1969(2003). 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; AE017180; AAR35751.1; -; Genomic_DNA. DR RefSeq; NP_953424.1; NC_002939.5. DR RefSeq; WP_010943014.1; NC_002939.5. DR AlphaFoldDB; Q74AH7; -. DR SMR; Q74AH7; -. DR STRING; 243231.GSU2378; -. DR EnsemblBacteria; AAR35751; AAR35751; GSU2378. DR KEGG; gsu:GSU2378; -. DR PATRIC; fig|243231.5.peg.2405; -. DR eggNOG; COG0135; Bacteria. DR HOGENOM; CLU_076364_2_0_7; -. DR InParanoid; Q74AH7; -. DR OrthoDB; 9796196at2; -. DR UniPathway; UPA00035; UER00042. DR Proteomes; UP000000577; Chromosome. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. 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..203 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT /id="PRO_1000071440" SQ SEQUENCE 203 AA; 21901 MW; 5578B6F52A577908 CRC64; MVRVKICGIT SLEDALVAVE AGADALGFVF HDESPRHVTP EQAAGIIAGL PPFIQTVGLF VNRPPAFVND TATRCRLDLV QLHGDEPPEF CDAVERRVIK AFRVKDISSL DPIRHYRVAA HLLDAYSPKA YGGTGLTFNW DIAAAAKAFG PLILAGGLTP DNVREAVETV KPYAVDVSGG VESAPGRKDA ARVREFIRRA KGW //