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Database: UniProt
Entry: A0A193GER7_9BORD
LinkDB: A0A193GER7_9BORD
Original site: A0A193GER7_9BORD 
ID   A0A193GER7_9BORD        Unreviewed;       218 AA.
AC   A0A193GER7;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|ARBA:ARBA00022272, ECO:0000256|HAMAP-Rule:MF_00135};
DE            Short=PRAI {ECO:0000256|HAMAP-Rule:MF_00135};
DE            EC=5.3.1.24 {ECO:0000256|ARBA:ARBA00012572, ECO:0000256|HAMAP-Rule:MF_00135};
GN   Name=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN   ORFNames=BAU07_16805 {ECO:0000313|EMBL:ANN78547.1};
OS   Bordetella flabilis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463014 {ECO:0000313|EMBL:ANN78547.1, ECO:0000313|Proteomes:UP000091926};
RN   [1] {ECO:0000313|EMBL:ANN78547.1, ECO:0000313|Proteomes:UP000091926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU10664 {ECO:0000313|EMBL:ANN78547.1,
RC   ECO:0000313|Proteomes:UP000091926};
RA   LiPuma J.J., Spilker T.;
RT   "Complete genome sequences of Bordetella bronchialis and Bordetella
RT   flabilis.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001164,
CC         ECO:0000256|HAMAP-Rule:MF_00135};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664,
CC       ECO:0000256|HAMAP-Rule:MF_00135}.
CC   -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00135}.
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DR   EMBL; CP016172; ANN78547.1; -; Genomic_DNA.
DR   RefSeq; WP_066659769.1; NZ_CP016172.1.
DR   AlphaFoldDB; A0A193GER7; -.
DR   STRING; 463014.BAU07_16805; -.
DR   KEGG; bfz:BAU07_16805; -.
DR   OrthoDB; 9796196at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000091926; 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 {ECO:0000256|HAMAP-Rule:MF_00135};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00135, ECO:0000313|EMBL:ANN78547.1};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT   DOMAIN          5..209
FT                   /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT                   /evidence="ECO:0000259|Pfam:PF00697"
SQ   SEQUENCE   218 AA;  23260 MW;  D574E51F925AEAAE CRC64;
     MRTRVKICGM TRPEDIATAI DAGADAVGLI FYPKSKRHVS LEQAARLRRA VPAFVDVVAL
     FVNPDDQTVR QVLDTVGPDL LQFHGEETPE DCERHGKRYL KAFRVGGPGA DTPARLGQTC
     AAFHGAAGWL FDSYTAGYGG SGLSFEHALL SEVRADPHGA ALILSGGLDP QNVGAAVTAL
     RPWAVDVSSG VEESPGLKSH ARIRAFLQAV RQADSDTK
//
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