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Database: UniProt
Entry: A0A0L0MAV3_9BURK
LinkDB: A0A0L0MAV3_9BURK
Original site: A0A0L0MAV3_9BURK 
ID   A0A0L0MAV3_9BURK        Unreviewed;       222 AA.
AC   A0A0L0MAV3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=BVER_03160c {ECO:0000313|EMBL:KND59852.1};
OS   Candidatus Burkholderia verschuerenii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=242163 {ECO:0000313|EMBL:KND59852.1, ECO:0000313|Proteomes:UP000036959};
RN   [1] {ECO:0000313|Proteomes:UP000036959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot4 {ECO:0000313|Proteomes:UP000036959};
RA   Carlier A., Eberl L., Pinto-Carbo M.;
RT   "Comparative genomics of Burkholderia leaf nodule symbionts.";
RL   Submitted (JUN-2015) 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|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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KND59852.1}.
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DR   EMBL; LFJJ01000095; KND59852.1; -; Genomic_DNA.
DR   RefSeq; WP_050454299.1; NZ_LFJJ01000095.1.
DR   AlphaFoldDB; A0A0L0MAV3; -.
DR   PATRIC; fig|242163.4.peg.267; -.
DR   OrthoDB; 9796196at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000036959; Unassembled WGS sequence.
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:KND59852.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036959};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT   DOMAIN          12..214
FT                   /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT                   /evidence="ECO:0000259|Pfam:PF00697"
SQ   SEQUENCE   222 AA;  23637 MW;  9E85A05FD9469E2F CRC64;
     MTDRDLHRTR IKLCGLSRQA DVEHAVELGA DAVGFVFYPP SPRSVSVSQA VELTRYVPPL
     VSSVGLFVNA TPEWIREVTS VVPLTLLQFH GDETPEQCAE LAAIAGLPYW RAVRVGPDAA
     ASDLLESSLN YAAADGILLD ALVEGFGGGG RVFDWSFIPT DLGHRAVLSG GLNAQNVSEA
     IRRVRPYAVD VSSGIEVPGA KGVKDPARMA AFVRAVRAAD AE
//
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