TRPF_METM7
ID TRPF_METM7 Reviewed; 208 AA.
AC A6VFU0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 65.
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=MmarC7_0246;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
RL Submitted (JUN-2007) 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: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; CP000745; ABR65316.1; -; Genomic_DNA.
DR RefSeq; WP_011976653.1; NC_009637.1.
DR AlphaFoldDB; A6VFU0; -.
DR SMR; A6VFU0; -.
DR STRING; 426368.MmarC7_0246; -.
DR EnsemblBacteria; ABR65316; ABR65316; MmarC7_0246.
DR GeneID; 5329553; -.
DR KEGG; mmz:MmarC7_0246; -.
DR eggNOG; arCOG01983; Archaea.
DR HOGENOM; CLU_076364_2_1_2; -.
DR OMA; HDHRISQ; -.
DR OrthoDB; 117266at2157; -.
DR UniPathway; UPA00035; UER00042.
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 Tryptophan biosynthesis.
FT CHAIN 1..208
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_1000057878"
SQ SEQUENCE 208 AA; 23247 MW; C5E34FF21C7A0926 CRC64;
MFIKICGIKT PEELEIVESY GNATGVILEC ASKRRIGLET AKNLVNLSNI PVFAVSTTSE
VLVWENIIKL TNTNYLQMHS DIDQKTIDFI KNEYGCFIMK SFKIPETSES PEIDAEKIIS
DIETYEVDRI LLDTGKGCGQ THDHRISQII AKKFDIILAG GLDPDNVFDI VKNVKPFGVD
VSSGVEANNS KDEELIKRFC ENVKSVKL