ID   TRPB_BUCAI              Reviewed;         388 AA.
AC   Q44685;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=BU278;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-340.
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; BA000003; BAB12988.1; -; Genomic_DNA.
DR   EMBL; L46355; AAC41536.1; -; Genomic_DNA.
DR   RefSeq; NP_240102.1; NC_002528.1.
DR   RefSeq; WP_010896041.1; NC_002528.1.
DR   AlphaFoldDB; Q44685; -.
DR   SMR; Q44685; -.
DR   STRING; 107806.10038953; -.
DR   EnsemblBacteria; BAB12988; BAB12988; BAB12988.
DR   KEGG; buc:BU278; -.
DR   PATRIC; fig|107806.10.peg.288; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_6; -.
DR   OMA; GPEHAMF; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001806; 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; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..388
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098926"
FT   MOD_RES         86
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        221
FT                   /note="K -> T (in Ref. 2; AAC41536)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   388 AA;  43084 MW;  178A6CA91128D480 CRC64;
     MTLLNPYFGE FGGMYVPQIL MPALFELEKN FVSAQKDAEF QKKFFYLLQN YAGRPTPLTL
     CKNLTKGTKT KIYLKREDLL HGGAHKTNQV LGQAMLAIRM KKKEIIAETG AGQHGVASAI
     ACALFNLKCR IYMGIKDIKR QNTNVFRMKL MGAEVISVKN GSGTLKDACN EALRDWSSSY
     KKSHYMIGTA AGPHPYPTIV REFQKMIGEE TKKQILEKEN KLPDSIIACI GGGSNAIGIF
     SDFINDKVNL IGVEPAGYGI HTGKHGAPLK HGRTGIYFGM KSHLMQNKQG QIQESWSISA
     GLDFPSVGPE HAWLNSINRA KYVSITDEEA ISAFQVLSRK EGIIPALESS HALAYALKLM
     KKDPTIEQIL IANLSVVEIK IFLQYMMF