ID   TRPB1_THEKO             Reviewed;         389 AA.
AC   Q9YGB0;
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 1 {ECO:0000255|HAMAP-Rule:MF_00133};
DE            EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00133};
GN   Name=trpB1 {ECO:0000255|HAMAP-Rule:MF_00133}; Synonyms=trpB;
GN   OrderedLocusNames=TK0257;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=10628865; DOI=10.1007/s004380051145;
RA   Tang X., Ezaki S., Fujiwara S., Takagi M., Atomi H., Imanaka T.;
RT   "The tryptophan biosynthesis gene cluster trpCDEGFBA from Pyrococcus
RT   kodakaraensis KOD1 is regulated at the transcriptional level and expressed
RT   as a single mRNA.";
RL   Mol. Gen. Genet. 262:815-821(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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}.
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DR   EMBL; AB030011; BAA82550.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD84446.1; -; Genomic_DNA.
DR   PIR; T43927; T43927.
DR   AlphaFoldDB; Q9YGB0; -.
DR   SMR; Q9YGB0; -.
DR   IntAct; Q9YGB0; 1.
DR   MINT; Q9YGB0; -.
DR   STRING; 69014.TK0257; -.
DR   EnsemblBacteria; BAD84446; BAD84446; TK0257.
DR   KEGG; tko:TK0257; -.
DR   PATRIC; fig|69014.16.peg.256; -.
DR   eggNOG; arCOG01433; Archaea.
DR   HOGENOM; CLU_016734_3_1_2; -.
DR   InParanoid; Q9YGB0; -.
DR   OMA; GPEHAMF; -.
DR   PhylomeDB; Q9YGB0; -.
DR   BioCyc; MetaCyc:MON-3562; -.
DR   BRENDA; 4.2.1.122; 5246.
DR   BRENDA; 4.2.1.20; 5246.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; 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..389
FT                   /note="Tryptophan synthase beta chain 1"
FT                   /id="PRO_0000099053"
FT   MOD_RES         85
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   389 AA;  42603 MW;  A7D95AAB114DF0CD CRC64;
     MDDMFFGRFG GQFVPETLIE PLKKLERAYK KFKDDPEFNE TLEYYLRNWA GRPTPLYYAE
     RLSKKLGGAK IYLKREDLLH GGAHKTNNGI GQALLAKFMG KERLIAETGA GQHGVATAMA
     GALLGMKVDV YMGAEDVERQ KMNVFRMGLL GARVIPVESG SRTLKDAINE ALRDWVATFE
     YSHYLIGSVV GPYPYPVIVR DFQSVIGREA REQILEAEGT LPDAVVACVG GGSNAMGIFY
     PFVNDRVRLI GVEAGGKGLE TGLHAASLNA GELGVFHGML SYFLQNEEGQ ITPTHSVSAG
     LDYPGVGPEH AYLKDSGRAE YVTVTDEEAL RAFHELSRTE GILPALESAH AVAYAMKIAP
     EMDKDEIIIV NLSGRGDKDL DIVRRVGNV