TRPF_PSEU5
ID TRPF_PSEU5 Reviewed; 207 AA.
AC A4VKF4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
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}; OrderedLocusNames=PST_1779;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RX PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Nitrogen fixation island and rhizosphere competence traits in the genome
RT of root-associated Pseudomonas stutzeri A1501.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP79455.1; -; Genomic_DNA.
DR RefSeq; WP_011912932.1; NC_009434.1.
DR AlphaFoldDB; A4VKF4; -.
DR SMR; A4VKF4; -.
DR STRING; 379731.PST_1779; -.
DR EnsemblBacteria; ABP79455; ABP79455; PST_1779.
DR KEGG; psa:PST_1779; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_2_0_6; -.
DR OMA; FYAKSPR; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000000233; 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..207
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_1000018627"
SQ SEQUENCE 207 AA; 21891 MW; B4C3D61FBB90DE6F CRC64;
MPVVRSKICG ITRVEDALIA AKAGADAIGL VFYGKSPRAV SLQRAREIVA ALPPFVTTVG
LFVNASRCEI NEILDAVPLD MLQFHGDESP AQCEGFHRPW YKALRVGGGE DIAAQVALYA
NASGVLLDTF VAGVPGGTGE CFDWSLIPPN LSKPLILAGG LTADNVEQAI AQVRPYAVDI
SGGVEASKGI KDAVKVETFV RRVRSVM