ID J3DNH1_9PSED Unreviewed; 206 AA.
AC J3DNH1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=PMI18_05189 {ECO:0000313|EMBL:EJL95636.1};
OS Pseudomonas sp. GM102.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144321 {ECO:0000313|EMBL:EJL95636.1, ECO:0000313|Proteomes:UP000007514};
RN [1] {ECO:0000313|EMBL:EJL95636.1, ECO:0000313|Proteomes:UP000007514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM102 {ECO:0000313|EMBL:EJL95636.1,
RC ECO:0000313|Proteomes:UP000007514};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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}.
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:EJL95636.1}.
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DR EMBL; AKJB01000116; EJL95636.1; -; Genomic_DNA.
DR RefSeq; WP_007905947.1; NZ_AKJB01000116.1.
DR AlphaFoldDB; J3DNH1; -.
DR PATRIC; fig|1144321.3.peg.5020; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000007514; 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:EJL95636.1};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 7..201
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 206 AA; 21492 MW; FA31522A7E41F077 CRC64;
MSAVRSKICG ITRIEDALAA VEAGADAIGF VFYAKSPRAV TFQQARAIIK ALPPFVTTVG
LFVNASRCEL GEILDAVPLD LLQFHGDETA ADCEGWHRPY IKALRVKAGD DIAAACDAYA
SASGILLDTY VEGVPGGTGE AFDWSLIPHG LSKPIILAGG LTPDNVAEAI ARVRPYAVDV
SGGVEASKGI KDHAKIQAFI KAVVGA
//
