TRPE_THEKO
ID TRPE_THEKO Reviewed; 433 AA.
AC Q9YGB3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=TK0254;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=10628865; DOI=10.1007/s004380051145;
RA Tang X., Ezaki S., Fujiwara S., Takagi M., Atomi H., Imanaka T.;
RT "The tryptophan biosynthesis gene cluster trpCDEGFBA from Pyrococcus
RT kodakaraensis KOD1 is regulated at the transcriptional level and expressed
RT as a single mRNA.";
RL Mol. Gen. Genet. 262:815-821(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC step biosynthesis of anthranilate, an intermediate in the biosynthesis
CC of L-tryptophan. In the first step, the glutamine-binding beta subunit
CC (TrpG) of anthranilate synthase (AS) provides the glutamine
CC amidotransferase activity which generates ammonia as a substrate that,
CC along with chorismate, is used in the second step, catalyzed by the
CC large alpha subunit of AS (TrpE) to produce anthranilate. In the
CC absence of TrpG, TrpE can synthesize anthranilate directly from
CC chorismate and high concentrations of ammonia (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00897};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00897};
CC -!- ACTIVITY REGULATION: Feedback inhibited by tryptophan. {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; AB030011; BAA82547.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD84443.1; -; Genomic_DNA.
DR PIR; T43924; T43924.
DR RefSeq; WP_011249209.1; NC_006624.1.
DR AlphaFoldDB; Q9YGB3; -.
DR SMR; Q9YGB3; -.
DR STRING; 69014.TK0254; -.
DR EnsemblBacteria; BAD84443; BAD84443; TK0254.
DR GeneID; 3235373; -.
DR KEGG; tko:TK0254; -.
DR PATRIC; fig|69014.16.peg.253; -.
DR eggNOG; arCOG02014; Archaea.
DR HOGENOM; CLU_006493_9_3_2; -.
DR InParanoid; Q9YGB3; -.
DR OMA; ETMGSVE; -.
DR OrthoDB; 13784at2157; -.
DR PhylomeDB; Q9YGB3; -.
DR BRENDA; 4.1.3.27; 5246.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR010116; Anthranilate_synth_I_arc_typ.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR01820; TrpE-arch; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Magnesium; Metal-binding; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..433
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154131"
FT BINDING 29
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 219..221
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 253..254
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 368
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 388
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 402..404
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 404
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 417
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
SQ SEQUENCE 433 AA; 48541 MW; E2C539B23365D599 CRC64;
MPLKKLKPVD PLKLYSALRD FGMPFMLRSA EKDSRKARFT YISAEPEFVV EVGEGTEIDG
ERVSDERNPL RALKGLMGER VEGRRFMGGF VGYVSYDSVH SIIGGKIEEP SVFGYYPWTF
IYDHSTGALS FFYLREAPFD PEALVERARR EESRLEDGGS EVISTDAGME EFVEIVRAGK
EYIYSGDVFQ VVLSREYRVR TDLDALEIYK RLVELNPSPY TFILEFEKTV VGASPETMGS
VEGRTFKINP IAGTAPRGRT GEEDRELEKA LLSDEKERAE HVMLVDLARN DVRRVSKPGS
VRLTRFFDVL KYSHVQHIES EVVGELDEGK NAFDAMEAAF PAGTLTGAPK IRAMEIIDEL
ERSRRKVYGG AVGYFSLTGD ADMAIAIRMA EIEGRKASVR AGAGIVADSV PEKEFFETEN
KMRAVLKALG VRE
