ID   TRPB_METVO              Reviewed;         409 AA.
AC   P14638;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB;
OS   Methanococcus voltae.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX   PubMed=3146017; DOI=10.1007/bf00330478;
RA   Sibold L., Henriquet M.;
RT   "Cloning of the trp genes from the archaebacterium Methanococcus voltae:
RT   nucleotide sequence of the trpBA genes.";
RL   Mol. Gen. Genet. 214:439-450(1988).
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; M35130; AAA72854.1; -; Genomic_DNA.
DR   AlphaFoldDB; P14638; -.
DR   SMR; P14638; -.
DR   UniPathway; UPA00035; UER00044.
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..409
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000099045"
FT   MOD_RES         92
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  44685 MW;  E0C5687591A56E6E CRC64;
     MKCNTKCDKN GYFGEFGGQY IPEVLKPAVE ELKEAYKELK DDEDFQNELA YYLKHYAGRE
     TPLYYAKNLT EKLGGAKIYL KREDLLHGGA HKTNNTIGQA LLAKKMGKTR IIAETGAGQH
     GVGTSMAGAL FGLETEIFMG RVDTERQQPN VARMKLLGAK VTPVDTGSKV LKDAVNEAMR
     NWTATFENTH YLLGTVMGPH PFPTMVRDFQ SVIGKEVKKQ IMEQEERLPD YLVACIGGGS
     NAMGLFHPFL SNNISTGNDD AKNVKMIGIE AAGKGLNTSL HGASITKGEK GVLHGMLSYF
     LQDEDGQIEE AYSISAGLDY PGIGPEHAYL HNLGRVQYAS ATDKQALKAF MELTRTEGII
     PALESSHAIA YAIENAGNMD KDDIMVINLS GRGDKDLNTV INAVHKLGC