ID   TRPF_DEHMC              Reviewed;         219 AA.
AC   Q3ZZ13;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, 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=cbdbA1447;
OS   Dehalococcoides mccartyi (strain CBDB1).
OC   Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=255470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBDB1;
RX   PubMed=16116419; DOI=10.1038/nbt1131;
RA   Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT   "Genome sequence of the chlorinated compound-respiring bacterium
RT   Dehalococcoides species strain CBDB1.";
RL   Nat. Biotechnol. 23:1269-1273(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; AJ965256; CAI83475.1; -; Genomic_DNA.
DR   RefSeq; WP_011309824.1; NC_007356.1.
DR   AlphaFoldDB; Q3ZZ13; -.
DR   SMR; Q3ZZ13; -.
DR   KEGG; deh:cbdbA1447; -.
DR   HOGENOM; CLU_076364_2_0_0; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000000433; 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   Tryptophan biosynthesis.
FT   CHAIN           1..219
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_1000018592"
SQ   SEQUENCE   219 AA;  23829 MW;  A07066BA5B10D916 CRC64;
     MIKTKICGLT EVGQALATAR TGADFAGVVF AESKRRITTE KALEIAEALK PLNPRPMLVG
     VFANQTAEEV NRIASVCRLD RVQLSGNESW EYCNQVNLPV IKVIHVAEST TAELVIQEIQ
     AGLKALKKTP VFLLDTHTKA LFGGSGQSFD WQIVKQVSLK YPVMVAGGLN PENIQGFIKI
     AKPWGIDVAS GVETDGIKDT AKIHLFIERV KDADGNRIC
//