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TRPB_BUCRM
ID   TRPB_BUCRM              Reviewed;         225 AA.
AC   Q44686;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
DE   Flags: Fragment;
GN   Name=trpB;
OS   Buchnera aphidicola subsp. Rhopalosiphum maidis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8642610; DOI=10.1007/bf02498635;
RA   Rouhbakhsh D., Lai C.-Y., von Dohlen C.D., Clark M.A., Baumann L.,
RA   Baumann P., Moran N.A., Voegtlin D.J.;
RT   "The tryptophan biosynthetic pathway of aphid endosymbionts (Buchnera):
RT   genetics and evolution of plasmid-associated anthranilate synthase (trpEG)
RT   within the aphididae.";
RL   J. Mol. Evol. 42:414-421(1996).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC         glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC         Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
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DR   EMBL; L46356; AAC41537.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q44686; -.
DR   SMR; Q44686; -.
DR   UniPathway; UPA00035; UER00044.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Pyridoxal phosphate; Tryptophan biosynthesis.
FT   CHAIN           <1..>225
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098931"
FT   NON_TER         1
FT   NON_TER         225
SQ   SEQUENCE   225 AA;  24660 MW;  ED6D2B4EA051CB7A CRC64;
     VAVSIACALF NLKCKIYMGY KDIKRQSPNV FRMKLMGAEV ISVRNGSGTL KDACNEALRD
     WSGNYQKSHY IIGTAAGPHP YPTIVKEFQK MIGEEAKKQI LEQEKKLPDA IIACVGGGSN
     AIGIFSEFMN EKVDLIGVEP AGRGIETGKH GAPLNHGRTG IYFGMKSSLM QNQEGQIEKS
     WSISAGLDFP SVGPEHAWLH SINRAQYVSI TDIEALEAFQ ILSKK
 
 
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