ID   TRPB2_THEKO             Reviewed;         442 AA.
AC   Q5JDJ1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Tryptophan synthase beta chain 2 {ECO:0000255|HAMAP-Rule:MF_00133};
DE            EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00133};
GN   Name=trpB2 {ECO:0000255|HAMAP-Rule:MF_00133}; OrderedLocusNames=TK1442;
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 [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; AP006878; BAD85631.1; -; Genomic_DNA.
DR   RefSeq; WP_011250393.1; NC_006624.1.
DR   AlphaFoldDB; Q5JDJ1; -.
DR   SMR; Q5JDJ1; -.
DR   STRING; 69014.TK1442; -.
DR   EnsemblBacteria; BAD85631; BAD85631; TK1442.
DR   GeneID; 3233674; -.
DR   KEGG; tko:TK1442; -.
DR   PATRIC; fig|69014.16.peg.1404; -.
DR   eggNOG; arCOG01432; Archaea.
DR   HOGENOM; CLU_042858_1_0_2; -.
DR   InParanoid; Q5JDJ1; -.
DR   OMA; MLHQTII; -.
DR   OrthoDB; 24741at2157; -.
DR   PhylomeDB; Q5JDJ1; -.
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: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..442
FT                   /note="Tryptophan synthase beta chain 2"
FT                   /id="PRO_0000099054"
FT   MOD_RES         110
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   442 AA;  49262 MW;  BA11E5877DA2B8BF CRC64;
     MKAVLPDSKI PKRWYNILPD LPEPLAPPLD PETDEPMEPE KLLRIFAEEL VKQEMSTDRY
     IEIPKEVREI YSKIGRPTPL FRATNLERAL GTPARIYFKY EGATVTGSHK INTALAQAYY
     AKRQGIERLV TETGAGQWGT ALSLAGALLG LNVRVYMARA SYQQKPYRKT IMRLYGAEIY
     PSPSDRTEIG RKFLAEDPNH PGGLGIAISE AIEDVLRDEK ARYALGSVLN HVLMHQTVIG
     LEAQEQMKEF EEPDVIIGCV GGGSNFAGLA YPFVRDVLKG EAEYEFIAVE PKAAPSMTRG
     VYKYDYGDSG GYTPKMKMHT LGHTYYVPPI HAGGLRYHGL APTLSVLINH GIVKPVAYHQ
     NEVFQAAHLF AKTEGIVPAP ESAHAIKGAI DRALEAKREG REEVILFNLS GHGFLDLKGY
     EDYLDGKLED YEPEHFPALD NY