ID   TRPF_SALRD              Reviewed;         221 AA.
AC   Q2S1Z4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=SRU_1668;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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}.
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DR   EMBL; CP000159; ABC45800.1; -; Genomic_DNA.
DR   RefSeq; WP_011404413.1; NC_007677.1.
DR   RefSeq; YP_445787.1; NC_007677.1.
DR   AlphaFoldDB; Q2S1Z4; -.
DR   SMR; Q2S1Z4; -.
DR   STRING; 309807.SRU_1668; -.
DR   EnsemblBacteria; ABC45800; ABC45800; SRU_1668.
DR   GeneID; 83728587; -.
DR   KEGG; sru:SRU_1668; -.
DR   PATRIC; fig|309807.25.peg.1730; -.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_076364_2_0_10; -.
DR   OrthoDB; 9786954at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000008674; 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_1000057881"
SQ   SEQUENCE   221 AA;  24045 MW;  CC19A8D5F240B21D CRC64;
     MGVELKVCGI TELEDARYLA GAGADYLGFV QHEESARYAP PALASDIIEW VHGPAPVGVF
     VNDGADTINE AVDTAGFELA QLHGQEPAHV VERVDCPVIK AIHVRHDAAP NQLRTLFERY
     EDGVEYFLLD THDSSVWGGT GESFNWRLAR ELAEDYPVFL AGGLNADNVA RALETMRPFA
     VDLSSSLESA PGQKSFEKID AFMDAFQAAA AELEEAETHD P
//