ID   TRPF2_METMA             Reviewed;         226 AA.
AC   Q8PRX4;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 2.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase 2;
DE            Short=PRAI 2;
DE            EC=5.3.1.24;
GN   Name=trpF2; OrderedLocusNames=MM_3314;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAM33010.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008384; AAM33010.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8PRX4; -.
DR   SMR; Q8PRX4; -.
DR   STRING; 192952.MM_3314; -.
DR   DNASU; 1481656; -.
DR   EnsemblBacteria; AAM33010; AAM33010; MM_3314.
DR   KEGG; mma:MM_3314; -.
DR   PATRIC; fig|192952.21.peg.3849; -.
DR   eggNOG; arCOG01983; Archaea.
DR   HOGENOM; CLU_076364_2_0_2; -.
DR   OMA; CEIMEIC; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000000595; 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; -; 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; Aromatic amino acid biosynthesis; Isomerase;
KW   Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..226
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase 2"
FT                   /id="PRO_0000154406"
SQ   SEQUENCE   226 AA;  24760 MW;  1EE6D057BEA7536E CRC64;
     MRIKVCGIKR VEDAVMAAYC GADAIGLVVG RKHNSDDFID KHLAQKIVRE CPPYISPVLV
     TELDDAEEIS GLVHETGVTS VQLHSDCTVD SIISLRKTFP NIKIIKNFHV IGPGVIHAMK
     PFESVVDAFI LDTLDLANDK VGSTGLVHDW SISRKIVKEV SRPVILAGGL TPENVGEAIR
     VVNPYGVDAS SGLKDSNGFK DEMKVINFVH RAKNDFFKVR NLSLEN