TRPB_BUCAP
ID TRPB_BUCAP Reviewed; 399 AA.
AC P42391;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Tryptophan synthase beta chain;
DE EC=4.2.1.20;
GN Name=trpB; OrderedLocusNames=BUsg_267;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8407819; DOI=10.1128/jb.175.20.6426-6432.1993;
RA Munson M.A., Baumann P.;
RT "Molecular cloning and nucleotide sequence of a putative trpDC(F)BA operon
RT in Buchnera aphidicola (endosymbiont of the aphid Schizaphis graminum).";
RL J. Bacteriol. 175:6426-6432(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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; Z19055; CAA79500.1; -; Genomic_DNA.
DR EMBL; AE013218; AAM67825.1; -; Genomic_DNA.
DR PIR; C49897; C49897.
DR RefSeq; WP_011053792.1; NC_004061.1.
DR AlphaFoldDB; P42391; -.
DR SMR; P42391; -.
DR STRING; 198804.BUsg_267; -.
DR EnsemblBacteria; AAM67825; AAM67825; BUsg_267.
DR KEGG; bas:BUsg_267; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_6; -.
DR OMA; HGMKSYF; -.
DR OrthoDB; 912282at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd06446; Trp-synth_B; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00263; trpB; 1.
DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Pyridoxal phosphate; Tryptophan biosynthesis.
FT CHAIN 1..399
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_0000098927"
FT MOD_RES 86
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 44247 MW; DEBFD45D2C859C30 CRC64;
MTLLNPYFGK FGGMYVPQIL MPALYQLEKN FVDAKKDSNF QKSFFNYLKN YAGRPTPLTL
CNNLTNGTKT RIYLKREDLL HGGAHKTNQV LGQAMLAVKM KKKEIIAETG AGQHGVAAAI
ASALFNLKCK IYMGYKDIKR QSPNVFRMKL MGAEVVSVES GSGTLKDACN EALRDWSRNY
QKSHYMIGTA AGPHPYPTIV KEFQKMIGEE AKKQILEQEN RLPDAIIACV GGGSNAIGIF
SDFIDEDVNL IGVEPAGQGI ETGKHGAPLN HGRTGIYFGM KSHLMQSQEG QIEKSWSISA
GLDFPSVGPE HSWLNSIHRA KYVSITDIEA LEAFQILSKK EGIIPALESS HALAYALKLM
YLDPKKEQVF IVNLSGRGDK DIFTVREILK KTEKKHESL