ID A0A8A3NA99_9HYPH Unreviewed; 222 AA. AC A0A8A3NA99; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 25-MAY-2022, entry version 3. DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|ARBA:ARBA00022272, ECO:0000256|HAMAP-Rule:MF_00135}; DE Short=PRAI {ECO:0000256|HAMAP-Rule:MF_00135}; DE EC=5.3.1.24 {ECO:0000256|ARBA:ARBA00012572, ECO:0000256|HAMAP-Rule:MF_00135}; GN Name=trpF {ECO:0000256|HAMAP-Rule:MF_00135}; GN ORFNames=J3O30_00105 {ECO:0000313|EMBL:QSZ21018.1}; OS Rhizobium sp. NZLR1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=2731096 {ECO:0000313|EMBL:QSZ21018.1}; RN [1] {ECO:0000313|EMBL:QSZ21018.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NZLR1 {ECO:0000313|EMBL:QSZ21018.1}; RA Gai Y., Riely B.; RT "Comparative genomic analysis of Rhizobium strains in Lentils."; RL Submitted (MAR-2021) 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:0000256|HAMAP-Rule:MF_00135}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664, CC ECO:0000256|HAMAP-Rule:MF_00135}. CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000256|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; CP071632; QSZ21018.1; -; Genomic_DNA. DR UniPathway; UPA00035; UER00042. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:InterPro. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:InterPro. DR CDD; cd00405; PRAI; 1. DR Gene3D; 3.20.20.70; -; 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; PTHR42894; 1. DR Pfam; PF00697; PRAI; 1. DR SUPFAM; SSF51366; SSF51366; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00135, ECO:0000313|EMBL:QSZ21018.1}; KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}. FT DOMAIN 6..208 FT /note="PRAI" FT /evidence="ECO:0000259|Pfam:PF00697" SQ SEQUENCE 222 AA; 23757 MW; 77EB62B9376FCF97 CRC64; MKPDIKICGL TTPDAVDRAL KRGATHIGFI FFEKSPRYIE PDLAAKLAEP ARGKAKIVAV VVDPTNDDLD EIVSLLKPDI LQLHGNESPE HVLTIKALYG LPVMKVFSVR TADDLKRVEA YIGIADRFLF DAKAPKGSEL PGGNGVSFDW SLLSWLDGSI DYMLSGGLNK NNVADALANT KARGIDVSSG VETAPGVKSV AMIDEFFDAV EEADAPVMAS GS //