ID   TRPF_GLOVI              Reviewed;         222 AA.
AC   Q7NML1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   02-SEP-2026, entry version 113.
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=gll0754;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Gloeobacterales;
OC   Gloeobacteraceae; Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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; BA000045; BAC88695.1; -; Genomic_DNA.
DR   RefSeq; WP_011140756.1; NC_005125.1.
DR   AlphaFoldDB; Q7NML1; -.
DR   SMR; Q7NML1; -.
DR   STRING; 251221.gene:10758231; -.
DR   EnsemblBacteria; BAC88695; BAC88695; BAC88695.
DR   KEGG; gvi:gll0754; -.
DR   PATRIC; fig|251221.4.peg.768; -.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_076364_2_0_3; -.
DR   InParanoid; Q7NML1; -.
DR   OrthoDB; 9786954at2; -.
DR   PhylomeDB; Q7NML1; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:L-tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00405; PRAI; 1.
DR   FunFam; 3.20.20.70:FF:000075; Tryptophan biosynthesis protein TRP1; 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   NCBIfam; NF002298; PRK01222.1-4; 1.
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..222
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_1000071441"
SQ   SEQUENCE   222 AA;  23553 MW;  7B1C75314CE9F640 CRC64;
     MRVKICGFTD PGQAQAAARL GVHALGFVCV PGTPRYVDAA RLREIAAALP PFTFKVGVFV
     DAPVEAMRAA VEAGELQGVQ LHGEESPETC AHLARTLPGI LRIKALRVRE PADLEKIALY
     VDAIEAVLLD AWHPTQAGGT GRTLDWKALQ GFCPALPWML SGGLRADNLA QALDILTPDA
     VDLSSGVENG VPGQKDLSKI TQILHIAQGN TGQRRPPLCD GT
//