ID Q9HK05_THEAC Unreviewed; 179 AA.
AC Q9HK05;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 107.
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 OrderedLocusNames=Ta0805 {ECO:0000313|EMBL:CAC11934.1};
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075 {ECO:0000313|EMBL:CAC11934.1, ECO:0000313|Proteomes:UP000001024};
RN [1] {ECO:0000313|EMBL:CAC11934.1, ECO:0000313|Proteomes:UP000001024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165
RC {ECO:0000313|Proteomes:UP000001024};
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.L., Koretke K.K., Volker C.,
RA Mewes H.W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; AL445065; CAC11934.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HK05; -.
DR STRING; 273075.gene:9572019; -.
DR PaxDb; 273075-Ta0805m; -.
DR EnsemblBacteria; CAC11934; CAC11934; CAC11934.
DR KEGG; tac:Ta0805; -.
DR eggNOG; arCOG01983; Archaea.
DR HOGENOM; CLU_076364_3_0_2; -.
DR InParanoid; Q9HK05; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000001024; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001024};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 4..168
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 179 AA; 19768 MW; DB074D2C590506C1 CRC64;
MLSDAGSDII GFVFDARSPR RSSYSTLKDA VASGIKTAAV YTDPASIMAS EMVEDFVQIH
FPHDRELIDY VHGQGRKVIS VIKYGIDDFM AKYREYGPAD IILVERKPKI SEIMGAEEFR
GKRIGFAGGI GTDDVERVIA EKPVMIDVSS SLESSPGHKD PEKVREFFSL VGGVHEPDR
//
