TRPE_BUCAI
ID TRPE_BUCAI Reviewed; 521 AA.
AC Q44695; Q9KGQ2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=BUpT01;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OG Plasmid pTrp (pBAp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8642610; DOI=10.1007/bf02498635;
RA Rouhbakhsh D., Lai C.-Y., von Dohlen C.D., Clark M.A., Baumann L.,
RA Baumann P., Moran N.A., Voegtlin D.J.;
RT "The tryptophan biosynthetic pathway of aphid endosymbionts (Buchnera):
RT genetics and evolution of plasmid-associated anthranilate synthase (trpEG)
RT within the aphididae.";
RL J. Mol. Evol. 42:414-421(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; L43555; AAD09346.1; -; Genomic_DNA.
DR EMBL; AP001070; BAA95417.1; -; Genomic_DNA.
DR RefSeq; NP_057962.1; NC_002252.1.
DR RefSeq; WP_010892289.1; NC_002252.1.
DR AlphaFoldDB; Q44695; -.
DR SMR; Q44695; -.
DR STRING; 107806.7707814; -.
DR EnsemblBacteria; BAA95417; BAA95417; BAA95417.
DR KEGG; buc:BUpT01; -.
DR PATRIC; fig|107806.10.peg.1; -.
DR eggNOG; COG0147; Bacteria.
DR HOGENOM; CLU_006493_9_4_6; -.
DR OMA; AYRSFMN; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000001806; Plasmid pTrp.
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; IEA:UniProtKB-UniPathway.
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; IPR005257; Anth_synth_I_TrpE.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR PANTHER; PTHR11236:SF22; PTHR11236:SF22; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PIRSF; PIRSF001373; TrpE; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00565; trpE_proteo; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Magnesium; Metal-binding; Plasmid; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..521
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154080"
FT BINDING 40
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 292..294
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 329..330
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 450
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 470
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 484..486
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 486
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT CONFLICT 1..10
FT /note="MFLIEKRRKL -> MQKSPYEIEI (in Ref. 1; AAD09346)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="D -> N (in Ref. 1; AAD09346)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 58793 MW; 1F09602A47F0E7C5 CRC64;
MFLIEKRRKL IQKKANYHSD PTTVFNHLCG SRPATLLLET AEVNKKNNLE SIMIVDSAIR
VSAVKNSVKI TALSENGAEI LSILKENPHK KIKFFEKNKS INLIFPSLDN NLDEDKKIFS
LSVFDSFRFI MKSVNNTKRT SKAMFFGGLF SYDLISNFES LPNVKKKQKC PDFCFYLAET
LLVVDHQKKT CLIQSSLFGR NVDEKNRIKK RTEEIEKKLE EKLTSIPKNK TTVPVQLTSN
ISDFQYSSTI KKLQKLIQKG EIFQVVPSRK FFLPCDNSLS AYQELKKSNP SPYMFFMQDE
DFILFGASPE SSLKYDEKNR QIELYPIAGT RPRGRKKDGT LDLDLDSRIE LEMRTNHKEL
AEHLMLVDLA RNDLARICEP GSRYVSDLVK VDKYSHVMHL VSKVVGQLKY GLDALHAYSS
CMNMGTLTGA PKVRAMQLIA EYEGEGRGSY GGAIGYFTDL GNLDTCITIR SAYVESGVAT
IQAGAGVVFN SIPEDEVKES LNKAQAVINA IKKAHFTMGS S
