TRPF_DESHY
ID TRPF_DESHY Reviewed; 237 AA.
AC Q24SK5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=DSY3198;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE84987.1; -; Genomic_DNA.
DR RefSeq; WP_011460913.1; NC_007907.1.
DR AlphaFoldDB; Q24SK5; -.
DR SMR; Q24SK5; -.
DR STRING; 138119.DSY3198; -.
DR EnsemblBacteria; BAE84987; BAE84987; DSY3198.
DR KEGG; dsy:DSY3198; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_2_0_9; -.
DR OMA; FYAKSPR; -.
DR OrthoDB; 1854712at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000001946; 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..237
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_1000018593"
SQ SEQUENCE 237 AA; 25749 MW; 9682C33BDE91280E CRC64;
MPRIKICGIR TGEEARWAVE AGADALGFIF VPHSKRYIQP ETAREIILNL PPLISKVGVF
AQASPEHVGR IVHECSLDTI QLHGNEDPRL YRHLSVTKIK AFSFPSAPAP GNSSEAAPDF
SLVETSPSSS LPTSFRELPP ASLHGILLDS SAGGRTGGTG IPLPWHTPVF QDFLHQVGDL
GYPLILAGGL NPDNILEAIR LTRPYGVDVS SGVERNGRKD REKIQHFISQ ARKESPL