TRPE_LACLA
ID TRPE_LACLA Reviewed; 456 AA.
AC Q02001;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=LL1470; ORFNames=L0054;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=1400208; DOI=10.1128/jb.174.20.6563-6570.1992;
RA Bardowski J., Ehrlich S.D., Chopin A.;
RT "Tryptophan biosynthesis genes in Lactococcus lactis subsp. lactis.";
RL J. Bacteriol. 174:6563-6570(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; M87483; AAA25223.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05568.1; -; Genomic_DNA.
DR PIR; F86808; F86808.
DR PIR; S35124; S35124.
DR RefSeq; NP_267626.1; NC_002662.1.
DR RefSeq; WP_003130425.1; NC_002662.1.
DR AlphaFoldDB; Q02001; -.
DR SMR; Q02001; -.
DR STRING; 272623.L0054; -.
DR PaxDb; Q02001; -.
DR EnsemblBacteria; AAK05568; AAK05568; L0054.
DR KEGG; lla:L0054; -.
DR PATRIC; fig|272623.7.peg.1580; -.
DR eggNOG; COG0147; Bacteria.
DR HOGENOM; CLU_006493_9_3_9; -.
DR OMA; GCVGYLD; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000002196; 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; 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; IPR005256; Anth_synth_I_PabB.
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; TIGR00564; trpE_most; 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..456
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154096"
FT BINDING 31
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 244..246
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 279..280
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 394
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 414
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 428..430
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 430
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT CONFLICT 164..165
FT /note="SA -> YR (in Ref. 1; AAA25223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 51676 MW; 32081A7640577B06 CRC64;
MRKIKEISAD TMTPISVYLR LKGKNKVILE SIPRENDQSR FSIIALNPVK HIKFTDGILS
VNDEIISDEN PMEFLEKLVC QPESTDENLD LPFTSGAIGY AGFDTYGIFE GIQPELKDSI
GTPDMYFMLY ESALIFDHKR EKLIFIEDNT YSQRSEKELQ NALSANIESL SLLTEAENEL
TELSKLNFVS NMSQELFEEK VAKAKELIRN GDMFQVVLSQ RLTADFTDNP FNYYRKLRVE
NPSSYMYFME FDNFHVIGSS PERLVAVHGN QVSTNPIAGT RKRGQTEFED QALIEDLESD
PKEVAEHKML VDLGRNDIGK ISKYGSIEVP VFMKVEKYRY VMHITSEVTG ELRPEFTAMD
ALRATLPAGT LSGAPKHRAY QRIYEFETQK RGIYGGAIGY LTKNGNCDFA IAIRTMVLKD
KKAHVQAGAG IVYDSVPEHE YQETLNKAQG LLKVGQ
