ID TRPF_STRR6 Reviewed; 199 AA. AC Q8DNM7; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 25-MAR-2003, sequence version 2. DT 24-JAN-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}; GN OrderedLocusNames=spr1633; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-255 / R6; RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001; RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). 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 -!- SEQUENCE CAUTION: CC Sequence=AAL00436.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AE007317; AAL00436.1; ALT_INIT; Genomic_DNA. DR PIR; G98075; G98075. DR RefSeq; NP_359225.1; NC_003098.1. DR RefSeq; WP_000169895.1; NC_003098.1. DR AlphaFoldDB; Q8DNM7; -. DR SMR; Q8DNM7; -. DR STRING; 171101.spr1633; -. DR KEGG; spr:spr1633; -. DR PATRIC; fig|171101.6.peg.1762; -. DR eggNOG; COG0135; Bacteria. DR HOGENOM; CLU_076364_1_0_9; -. DR UniPathway; UPA00035; UER00042. DR Proteomes; UP000000586; 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..199 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT /id="PRO_0000154387" SQ SEQUENCE 199 AA; 21366 MW; FC33273F9E4E8182 CRC64; MTKVKICGLS TKEAVETAVS AGADYIGFVF APSKRQVTLE EAAELAKLIP ADVKKVGVFV SPSRVELLEA IDKVGLDLVQ VHGQVADDLF ENLPCASIQA VQVDGNGHVP NSQADYLLFD APVAGSGQPF DWGQLDTTGL AQPFFIAGGL NEDNVVKAIQ HFTPYAVDVS SGVETDGQKD HEKIRRFIER VKNGISRTK //