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TRPE_PSEPU
ID   TRPE_PSEPU              Reviewed;         493 AA.
AC   P20579;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Anthranilate synthase component 1;
DE            Short=AS;
DE            Short=ASI;
DE            EC=4.1.3.27;
GN   Name=trpE;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 23287 / C1S;
RX   PubMed=2404959; DOI=10.1128/jb.172.2.867-883.1990;
RA   Essar D.W., Eberly L., Crawford I.P.;
RT   "Evolutionary differences in chromosomal locations of four early genes of
RT   the tryptophan pathway in fluorescent pseudomonads: DNA sequences and
RT   characterization of Pseudomonas putida trpE and trpGDC.";
RL   J. Bacteriol. 172:867-883(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.
CC       {ECO:0000269|PubMed:2404959}.
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   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow.
CC       {ECO:0000269|PubMed:2404959}.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC       {ECO:0000305}.
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DR   EMBL; M33799; AAA80551.1; -; Genomic_DNA.
DR   PIR; E35115; E35115.
DR   AlphaFoldDB; P20579; -.
DR   SMR; P20579; -.
DR   STRING; 1240350.AMZE01000023_gene1384; -.
DR   PRIDE; P20579; -.
DR   eggNOG; COG0147; Bacteria.
DR   SABIO-RK; P20579; -.
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..493
FT                   /note="Anthranilate synthase component 1"
FT                   /id="PRO_0000154107"
FT   BINDING         48
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         273..275
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         308..309
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         335
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         423
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         443
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         457..459
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         459
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         472
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
SQ   SEQUENCE   493 AA;  54449 MW;  FBD05348D0D94A76 CRC64;
     MNREEFLRLA AVGYNRIPLA CETLADFDTP LSIYLKLADQ PNSYLLESVQ GGEKWGRYSM
     IGLPSRTVMR VHGYHVSILH DGVEVESHDV EDPLAFVESF KDRYKVADIP GLPRFNGGLV
     GYFGYDCVRY VEKRLGVSPN PDPLGVPDIL LMVSDAVVVF DNLAGKMHAI VLVDPAEEQA
     FEQGQARLQG LLETLRQPIT PRRGLDLSGP QAAEPEFRSS YTREDYENAV GRIKEYILAG
     DCMQVVPSQR MSIDFKAAPI DLYRALRCFN PTPYMYFFNF GDFHVVGSSP EVLVRVEDNL
     VTVRPIAGTR PRGATEEADR ALEDDLLSDD KEIAEHLMLI DLGRNDVGRV SSTGSVRLTE
     KMVIERYSNV MHIVSNVAGQ LREGLTAMDA LRAILPAGTL SGAPKIRAME IIDELEPVKR
     GVYGGAVGYF AWNGNMDTAI AIRTAVINDG ELHVQAGGGI VADSVPALEW EETINKRRAM
     FRAVALAEQT SAK
 
 
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