ID M4YMT5_THEXX Unreviewed; 199 AA.
AC M4YMT5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|HAMAP-Rule:MF_00135};
DE Short=PRAI {ECO:0000256|HAMAP-Rule:MF_00135};
DE EC=5.3.1.24 {ECO:0000256|HAMAP-Rule:MF_00135};
GN Name=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN ORFNames=TALC_01438 {ECO:0000313|EMBL:AGI48415.1};
OS Thermoplasmatales archaeon (strain BRNA1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales.
OX NCBI_TaxID=1054217 {ECO:0000313|EMBL:AGI48415.1, ECO:0000313|Proteomes:UP000012076};
RN [1] {ECO:0000313|EMBL:AGI48415.1, ECO:0000313|Proteomes:UP000012076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRNA1 {ECO:0000313|EMBL:AGI48415.1,
RC ECO:0000313|Proteomes:UP000012076};
RA Denman S.E., Evans P., Bragg L., Padmanahba J., McKenzie M., Edwards D.,
RA Krzycki J., McSweeney C., Morrison M.;
RT "Thermoplasmatales-like gut symbionts are pyrrolysine dependent-
RT methanogens.";
RL Submitted (JUL-2011) 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: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|ARBA:ARBA00007571,
CC ECO:0000256|HAMAP-Rule:MF_00135}.
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DR EMBL; CP002916; AGI48415.1; -; Genomic_DNA.
DR AlphaFoldDB; M4YMT5; -.
DR STRING; 1054217.TALC_01438; -.
DR KEGG; tar:TALC_01438; -.
DR PATRIC; fig|1054217.5.peg.1369; -.
DR eggNOG; arCOG01983; Archaea.
DR HOGENOM; CLU_076364_1_0_2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000012076; 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; 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:AGI48415.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012076};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 4..188
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 199 AA; 22270 MW; FDD58D7E6E8358E5 CRC64;
MTRVKICGLR RREDAEYCNR YGADYAGFVF WKGSRRFVSP AAAKDVSDNL LPRIVPVGVF
VDEDVRVISS IADSGTIRMV QLHGDEDQEY IDLLRENVNI PIIRAYRPGC SRRFHADYSM
FDGGAGDGKT FDWSSLKDVH GPFFLAGGLS AENVPDAIRT LRPFAVDVST GVETDGYKDP
EKIRLFIEAV RKADAELEE
//
