ID   TRPB2_SULTO             Reviewed;         431 AA.
AC   Q970N1;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Tryptophan synthase beta chain 2;
DE            EC=4.2.1.20;
GN   Name=trpB2; OrderedLocusNames=STK_15670;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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; BA000023; BAB66642.1; -; Genomic_DNA.
DR   RefSeq; WP_010979620.1; NC_003106.2.
DR   AlphaFoldDB; Q970N1; -.
DR   SMR; Q970N1; -.
DR   STRING; 273063.STK_15670; -.
DR   EnsemblBacteria; BAB66642; BAB66642; STK_15670.
DR   GeneID; 1459606; -.
DR   KEGG; sto:STK_15670; -.
DR   PATRIC; fig|273063.9.peg.1785; -.
DR   eggNOG; arCOG01432; Archaea.
DR   OrthoDB; 24741at2157; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001015; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
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; 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..431
FT                   /note="Tryptophan synthase beta chain 2"
FT                   /id="PRO_0000099058"
FT   MOD_RES         111
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   431 AA;  48335 MW;  CF060126FC5FCD1D CRC64;
     MLEKVRFDLP QDEIPTEWYN ILPDLPEPLP EPQDPTGKSF EILKQVLPSK VLELEFSKER
     YIKIPEEVLQ RYLQVGRPTP IIRARKLEEY LGGYIKIYMK MESHTYTGSH KINSALAHVY
     FAKLDNAKFV STETGAGQWG SAVALASALF NIQAHIFMVR TSYYAKPYRR YLMQMYNAQV
     HPSPSEFTRY GREVLAKDPN TPGSLGIAIS EAVYYALENG GKYVVGSVVN SDILFKTIAG
     MEAKKQMEMI GEDPDYIIGV VGGGSNYAAL AYPFLGEELR KGKVRRKYIA SGAIEVPKMT
     KGVYKYDYPD TAKILPMLKM YTIGSDFIPA PVYAGGLRYH AVAPTLSLLM YKGIVQARDY
     SQEEAFSWAK LFSQIEGWVP APETSHALPI LKEIVEEAKK SGEKKTVLIS FSGHGLLDLA
     NYADVLGFNK E