TRPE_BACPU
ID TRPE_BACPU Reviewed; 513 AA.
AC P18267;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE;
OS Bacillus pumilus (Bacillus mesentericus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1408;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RUB502;
RX PubMed=2110100; DOI=10.1016/0378-1119(90)90497-f;
RA Rivas M.V., Jarvis E.D., Rudner R.;
RT "The structure of the trpE, trpD and 5' trpC genes of Bacillus pumilus.";
RL Gene 87:71-78(1990).
RN [2]
RP ERRATUM OF PUBMED:2110100.
RX PubMed=2227447; DOI=10.1016/0378-1119(90)90483-8;
RA Rivas M.V., Jarvis E.D., Rudner R.;
RL Gene 94:141-143(1990).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB02272.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M36468; AAB02272.1; ALT_INIT; Genomic_DNA.
DR PIR; JH0098; JH0098.
DR AlphaFoldDB; P18267; -.
DR SMR; P18267; -.
DR UniPathway; UPA00035; UER00040.
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; Tryptophan biosynthesis.
FT CHAIN 1..513
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154077"
FT BINDING 50
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 279..281
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 314..315
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 429
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 449
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 463..465
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 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
SQ SEQUENCE 513 AA; 58091 MW; 0E6B19904421CC5A CRC64;
MNSQSNLTQF LKDSESYKTI PIVETITVDT LSPIQIVEKL KQDIVYLLES KDESSSWSRY
SFIGLHPFLT LHDDQNKYIA RDAAGQKLMQ KQELKELLDW MKEQYQIKTP DIDIPFTGGA
VGYLSYDLIP TLTSVRPHRS ASTIENAHIC LPTMIAFDHE TNHVHFIQYT QLTGHETEDE
KIRAYKEKQK QLEQMIHKLH SKVDMKELIL SGNMNEPPSF EHVTSTYEKA QFLKDVEKIK
EYIRAGDIFQ GVLSQRFDIP VSVSSFELYR VLRIVNPSPY MYFMKLKDRD LVGSSPERLI
HAKNGHLEIH PIAGTRKRGT TREEDAELAR ELLEDEKEKA EHYMLVDLAR NDVGRVAEYG
SVSVPTFTKV VNFSHVMHII SIVTGKLKRD THPVDALMSA FPAGTLTGAP KIRAMQLLNE
MEPEPRETYG GCIAYIGFDG NIDSCITIRT MSVKNHTASI QAGAGIVADS VPENEWEETC
NKAGALLKAI QLAEHIFSEK ESVQDESPTI SSC
