ID TRPF_HALVD Reviewed; 221 AA. AC P52563; D4GT39; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase; DE Short=PRAI; DE EC=5.3.1.24; GN Name=trpF; OrderedLocusNames=HVO_2455; OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales; OC Haloferacaceae; Haloferax. OX NCBI_TaxID=309800; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DS2 / DSM 5716 / WFD11; RX PubMed=1537810; DOI=10.1128/jb.174.5.1694-1697.1992; RA Lam W.L., Logan S.M., Doolittle W.F.; RT "Genes for tryptophan biosynthesis in the halophilic archaebacterium RT Haloferax volcanii: the trpDFEG cluster."; RL J. Bacteriol. 174:1694-1697(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / RC VKM B-1768 / DS2; RX PubMed=20333302; DOI=10.1371/journal.pone.0009605; RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R., RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J., RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.; RT "The complete genome sequence of Haloferax volcanii DS2, a model RT archaeon."; RL PLoS ONE 5:E9605-E9605(2010). 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; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. CC -!- SIMILARITY: Belongs to the TrpF family. {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; M83788; AAA73176.1; -; Genomic_DNA. DR EMBL; CP001956; ADE04719.1; -; Genomic_DNA. DR RefSeq; WP_004042369.1; NZ_AOHU01000044.1. DR AlphaFoldDB; P52563; -. DR SMR; P52563; -. DR STRING; 309800.HVO_2455; -. DR PaxDb; 309800-C498_07575; -. DR EnsemblBacteria; ADE04719; ADE04719; HVO_2455. DR GeneID; 8924041; -. DR KEGG; hvo:HVO_2455; -. DR eggNOG; arCOG01983; Archaea. DR HOGENOM; CLU_076364_2_1_2; -. DR OrthoDB; 27513at2157; -. DR UniPathway; UPA00035; UER00042. DR Proteomes; UP000008243; 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..221 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT /id="PRO_0000154401" SQ SEQUENCE 221 AA; 22634 MW; 396453808C71FBAD CRC64; MTRVKVCGVT DETDLAAVDA AGADAVGAIC DVPVDTPREI PRERARELFA AAPPFLTTTL VTMPDSVDHA RDLAREVGPD VLQLHGDFAA DDLDSLRATG VGVVPVVDAT DLARARDLAP VVDAILVDTP SDSGAGGTGE THDWDASRDL VAAVDAPVIL AGGLTPDNVV EAVRTVEPYG VDVASGVEAS GGVKDHDAVR AFVAAAKTAR GAVDDHEEVV A //