TRPE_CORGL
ID TRPE_CORGL Reviewed; 518 AA.
AC P06557;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=Cgl3029, cg3359;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3808947; DOI=10.1093/nar/14.24.10113;
RA Matsui K., Sano K., Ohtsubo E.;
RT "Complete nucleotide and deduced amino acid sequences of the Brevibacterium
RT lactofermentum tryptophan operon.";
RL Nucleic Acids Res. 14:10113-10114(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=2263476; DOI=10.1093/nar/18.23.7138;
RA Heery D.M., Dunican L.K.;
RT "Nucleotide sequence of the Corynebacterium glutamicum trpE gene.";
RL Nucleic Acids Res. 18:7138-7138(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-275.
RX PubMed=3609747; DOI=10.1016/0378-1119(87)90007-2;
RA Sano K., Matsui K.;
RT "Structure and function of the trp operon control regions of Brevibacterium
RT lactofermentum, a glutamic-acid-producing bacterium.";
RL Gene 53:191-200(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
RX PubMed=3667535; DOI=10.1128/jb.169.11.5330-5332.1987;
RA Matsui K., Miwa K., Sano K.;
RT "Two single-base-pair substitutions causing desensitization to tryptophan
RT feedback inhibition of anthranilate synthase and enhanced expression of
RT tryptophan genes of Brevibacterium lactofermentum.";
RL J. Bacteriol. 169:5330-5332(1987).
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; X04960; CAA28623.1; -; Genomic_DNA.
DR EMBL; X55994; CAA39467.1; -; Genomic_DNA.
DR EMBL; BA000036; BAC00424.1; -; Genomic_DNA.
DR EMBL; BX927157; CAF18969.1; -; Genomic_DNA.
DR EMBL; M16663; AAA83989.1; -; Genomic_DNA.
DR EMBL; M17892; AAB59111.1; -; Genomic_DNA.
DR PIR; B24723; B24723.
DR RefSeq; NP_602223.1; NC_003450.3.
DR RefSeq; WP_011015581.1; NC_006958.1.
DR AlphaFoldDB; P06557; -.
DR SMR; P06557; -.
DR STRING; 196627.cg3359; -.
DR KEGG; cgb:cg3359; -.
DR KEGG; cgl:Cgl3029; -.
DR PATRIC; fig|196627.13.peg.2964; -.
DR eggNOG; COG0147; Bacteria.
DR HOGENOM; CLU_006493_9_4_11; -.
DR OMA; HARFSFV; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000582; 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; 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; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..518
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154091"
FT BINDING 38
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 283..285
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 324..325
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 445
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 465
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 479..481
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 481
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 494
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT CONFLICT 16
FT /note="E -> A (in Ref. 6; AAB59111)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="A -> T (in Ref. 1; CAA28623, 2; CAA39467, 5;
FT AAA83989 and 6; AAB59111)"
FT /evidence="ECO:0000305"
FT CONFLICT 357..358
FT /note="EH -> DD (in Ref. 1; CAA28623 and 2; CAA39467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 56384 MW; 0662D4A660C16FF5 CRC64;
MSTNPHVFSL DVRYHEDASA LFAHLGGTTA DDAALLESAD ITTKNGISSL AVLKSSVRIT
CTGNTVVTQP LTDSGRAVVA RLTQQLGQYN TAENTFSFPA SDAVDERERL TAPSTIEVLR
KLQFESGYSD ASLPLLMGGF AFDFLETFET LPAVEESVNT YPDYQFVLAE IVLDINHQDQ
TAKLAGVSNA PGELEAELNK LSLLIDAALP ATEHAYQTTP HDGDTLRVVA DIPDAQFRTQ
INELKENIYN GDIYQVVPAR TFTAPCPDAF AAYLQLRATN PSPYMFYIRG LNEGRSYELF
GASPESNLKF TAANRELQLY PIAGTRPRGL NPDGSINDEL DIRNELDMRT DAKEIAEHTM
LVDLARNDLA RVSVPASRRV ADLLQVDRYS RVMHLVSRVT ATLDPELDAL DAYRACMNMG
TLTGAPKLRA MELLRGVEKR RRGSYGGAVG YLRGNGDMDN CIVIRSAFVQ DGVAAVQAGA
GVVRDSNPQS EADETLHKAY AVLNAIALAA GSTLEVIR
