TRPF_SYNWW
ID TRPF_SYNWW Reviewed; 204 AA.
AC Q0B004;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=Swol_0360;
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen;
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI67700.1; -; Genomic_DNA.
DR RefSeq; WP_011639808.1; NC_008346.1.
DR AlphaFoldDB; Q0B004; -.
DR SMR; Q0B004; -.
DR STRING; 335541.Swol_0360; -.
DR EnsemblBacteria; ABI67700; ABI67700; Swol_0360.
DR KEGG; swo:Swol_0360; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_1_0_9; -.
DR OMA; FYAKSPR; -.
DR OrthoDB; 1789381at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000001968; 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..204
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_1000018644"
SQ SEQUENCE 204 AA; 22787 MW; 11AA5180B5488C05 CRC64;
MTRVKICGIR SLEEAIAARE AGAWAIGQVF APSPRRLEVD IAAAINRELG QSILKIGVFV
NEEAENLRRI VASCRLDMVQ LHGDEEPAYL EEVSVPVIKS FRVRGSLELE QLKRWRPWAY
LFDSYHPGVY GGTGESFDWS FLQEIARQER IILAGGLNTE NVGRAIHQLR PLVVDVSSGV
EYPSGGKDPA KIREFINIVQ EQAT