ID   TRPB2_THEMA             Reviewed;         422 AA.
AC   Q9WZ09;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Tryptophan synthase beta chain 2;
DE            EC=4.2.1.20;
GN   Name=trpB2; OrderedLocusNames=TM_0539;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; AE000512; AAD35624.1; -; Genomic_DNA.
DR   PIR; H72363; H72363.
DR   RefSeq; NP_228349.1; NC_000853.1.
DR   RefSeq; WP_004081366.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WZ09; -.
DR   SMR; Q9WZ09; -.
DR   STRING; 243274.THEMA_01980; -.
DR   EnsemblBacteria; AAD35624; AAD35624; TM_0539.
DR   KEGG; tma:TM0539; -.
DR   eggNOG; COG1350; Bacteria.
DR   InParanoid; Q9WZ09; -.
DR   OMA; MLHQTII; -.
DR   OrthoDB; 912282at2; -.
DR   BioCyc; MetaCyc:MON-3543; -.
DR   SABIO-RK; Q9WZ09; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0052684; F:L-serine hydro-lyase (adding indole, L-tryptophan-forming) activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..422
FT                   /note="Tryptophan synthase beta chain 2"
FT                   /id="PRO_0000099014"
FT   MOD_RES         111
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   422 AA;  46387 MW;  1A32AE27E22B5A8D CRC64;
     MRIVVNLKPE EIPKHWYNVL ADLPFKLDPP LDPETKQPIS PEKLSVIFPM SLIEQEVSEE
     RFIEIPEPVL KEYAVYRPTP LIRATFLEEY LQTPARIYYK YEGVSPTGSH KPNTAIAQAY
     YNKIEGVKRL VTETGAGQWG SALSYAGAKF GLEVKVFMVK VSYQQKPMRK YMMNLFGGKV
     TPSPSEETNF GRKILSEDPD NPGSLGIAIS EALEVAVSDP NTKYSLGSVL NHVLLHQTVI
     GLEIKKQLEL IGEKPDILLG CHGGGSNFGG TILPFVPDKL SGRDIRFVAC EPAACPSLTK
     GNYDYDFGDT AGLTPLLKMY TLGKDFIPPK IHAGGLRYHG SAPIIARLVK EGLVEAQAFD
     QDETFEAAKI FAKLEGIIPA PESAHAIAGA IREAKKAKEE GKERVIVFTL SGHGLLDLTA
     YV