ID   TRPB_THEON              Reviewed;         443 AA.
AC   B6YSU5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Tryptophan synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00133};
DE            EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00133};
GN   Name=trpB {ECO:0000255|HAMAP-Rule:MF_00133}; OrderedLocusNames=TON_0147;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000255|HAMAP-Rule:MF_00133}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000855; ACJ15632.1; -; Genomic_DNA.
DR   RefSeq; WP_012571105.1; NC_011529.1.
DR   AlphaFoldDB; B6YSU5; -.
DR   SMR; B6YSU5; -.
DR   STRING; 523850.TON_0147; -.
DR   EnsemblBacteria; ACJ15632; ACJ15632; TON_0147.
DR   GeneID; 7017801; -.
DR   KEGG; ton:TON_0147; -.
DR   PATRIC; fig|523850.10.peg.147; -.
DR   eggNOG; arCOG01432; Archaea.
DR   HOGENOM; CLU_042858_1_0_2; -.
DR   OMA; MLHQTII; -.
DR   OrthoDB; 24741at2157; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002727; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; IPR006316; Trp_synth_b-like.
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   PANTHER; PTHR48077:SF6; PTHR48077:SF6; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR   PIRSF; PIRSF500824; TrpB_prok; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01415; trpB_rel; 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..443
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_1000095831"
FT   MOD_RES         110
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   443 AA;  49198 MW;  F120B93453F5D575 CRC64;
     MKAVLPDSKM PKRWYNILPD LPEPLAPPLD PETDEPMESE KLLRIFASEL VKQEMSMERY
     IDIPKKVREL YAKIGRPTPL FRATNLEKAL ETPARIYFKY EGATVTGSHK INTALAQAYY
     AKKQGIERLV TETGAGQWGT ALSLAGALMG INVRVYMARA SFYQKPYRKT IMRLYGAEIY
     PSPSDRTEIG RKFLSEDPNH PGGLGIAISE AIEDVLRDEK ARYALGSVLN HVLMHQTVIG
     LEAKEQMKEF EDPDVIIGCV GGGSNFAGLA YPFVKDRLDG KADYEFIAVE PRAAPSMTRG
     VYTYDYGDSG GLTPKMKMHT LGHTYYVPPI HAGGLRYHGL APTLSILINH GIVRPVAYHQ
     TEVFEAARLF AKTEGIVPAP ESAHAVKAAI DRALKAKEEG KEEVILFNLS GHGLLDLKGY
     EDFLDGKLED YEPEELPALR GEV