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TRPE_BUCSC
ID   TRPE_BUCSC              Reviewed;         530 AA.
AC   Q44598;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, 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   Buchnera aphidicola subsp. Schlechtendalia chinensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7742976; DOI=10.1111/j.1365-2583.1995.tb00007.x;
RA   Lai C.-Y., Baumann P., Moran N.A.;
RT   "Genetics of the tryptophan biosynthetic pathway of the prokaryotic
RT   endosymbiont (Buchnera) of the aphid Schlechtendalia chinensis.";
RL   Insect Mol. Biol. 4:47-59(1995).
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; U09184; AAC31215.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q44598; -.
DR   SMR; Q44598; -.
DR   STRING; 118110.XW81_02705; -.
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; 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; Tryptophan biosynthesis.
FT   CHAIN           1..530
FT                   /note="Anthranilate synthase component 1"
FT                   /id="PRO_0000154087"
FT   BINDING         40
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         290..292
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         327..328
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         360
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         448
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         468
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         482..484
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         484
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         497
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
SQ   SEQUENCE   530 AA;  60189 MW;  2AE8702A6DBE7AB5 CRC64;
     MCEHLKSMDV LKVETFYQPN PTAIFHHICR NRSNTLLLES AEINNKKNLE SMMIVDSALR
     ISALNMVVTL EALTKNGESL LPVFKSLLPK EVRILSNDNF LKIKFPSIVK DIDEDKKLHV
     LSIFDSIRFL INSVKNNKGS KSMFFGGLFA YDLVSSFENL PKLKTSQSCP DFCFYLSEIL
     LVLNHKRRTC YIQASLFSSS NLERNKLQHR LLEVKNKLSQ NFYPLESTSL KKMILKCNRT
     DREYEKIIKE MKKSIMIGEI FQVVPSRKFY LPCTNSLAAY DVLKKNNPSP YMFFMQDSNF
     TLFGASPESS LKYDTLSRKI EIYPIAGTRP RARKIDGSID LDLDSRIELE MRTNHKELSE
     HLMLVDLARN DLAKICDPGT RYVADLTQVD KYSHVMHLVS RVVGKLRLDL DVFHAYQACM
     NMGTLSGAPK IRAMELISNA EKEKRGSYGG SIGYFTASGT LDMCIIIRSA YVENNIATIQ
     VGAGIVLDSI PQLEVDESKN KAKAVLQAIS ESHSCHIELN IENERHTFAG
 
 
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