TRPE_CITFR
ID TRPE_CITFR Reviewed; 150 AA.
AC P00896;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
DE Flags: Fragment;
GN Name=trpE;
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6749821; DOI=10.1128/jb.152.1.57-62.1982;
RA Blumenberg M., Yanofsky C.;
RT "Evolutionary divergence of the Citrobacter freundii tryptophan operon
RT regulatory region: comparison with other enteric bacteria.";
RL J. Bacteriol. 152:57-62(1982).
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; J01557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01116; NNEB1C.
DR AlphaFoldDB; P00896; -.
DR SMR; P00896; -.
DR UniPathway; UPA00035; UER00040.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
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; IPR005257; Anth_synth_I_TrpE.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR PANTHER; PTHR11236:SF22; PTHR11236:SF22; 1.
DR SUPFAM; SSF56322; SSF56322; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Tryptophan biosynthesis.
FT CHAIN 1..>150
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154089"
FT BINDING 40
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 119
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT NON_TER 150
SQ SEQUENCE 150 AA; 16187 MW; 7E6B8E7F3DE6DDAF CRC64;
MQTQKPTLEL VACDAAYREN PTALFHQVCG ARPATLLLES ADIDSKDDLK SLLLVDSALR
ITAIGDTVTI QALSANGASL LPLLDAALPA GVENKQQPNG RHLRFPAVSP LLDEDVRLRS
LSAPDAFRPL QELVNVPAQE REVMFLGGMF
