ID   TRPB_PICTO              Reviewed;         419 AA.
AC   Q6L271;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=PTO0346;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT42931.1; -; Genomic_DNA.
DR   RefSeq; WP_011177147.1; NC_005877.1.
DR   AlphaFoldDB; Q6L271; -.
DR   SMR; Q6L271; -.
DR   STRING; 263820.PTO0346; -.
DR   PRIDE; Q6L271; -.
DR   EnsemblBacteria; AAT42931; AAT42931; PTO0346.
DR   GeneID; 2844845; -.
DR   KEGG; pto:PTO0346; -.
DR   PATRIC; fig|263820.9.peg.368; -.
DR   eggNOG; arCOG01432; Archaea.
DR   HOGENOM; CLU_042858_1_0_2; -.
DR   OMA; QWGMAVS; -.
DR   OrthoDB; 24741at2157; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000438; 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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..419
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000099046"
FT   MOD_RES         113
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   419 AA;  46228 MW;  70935A892467EA66 CRC64;
     MSEEFKSLLS SDIIPENWYN VTPDLPEPLP PPRDTKSDFS SINLLNKILP KEVLKQEFTF
     KRYEKIPDEI IDKYIQIGRP TPLIRAKNLE KYLDYGGKIF FKFEGATATG SHKINTAIAQ
     AYYAMNENAN GVTTETGAGQ WGSATALAAS LYNLKSQIFM VRVSYEQKPL RKVVMSLYNS
     SVVPSPSNLT EFGRKILSEN PDHPGTLGIG ISEAVEYALD HNYRYMVASV MNAALTHQSV
     IGQESIKQME LLGEFPDVLF GCVGGGSNFG GFAFPFLPIN DDIEIYATTA QEVPKFSQGE
     YKYDLMDTAG VLPAVRMYSL GADFVPPKIY AGGLRYHGAA PSLSLLINHG RIKSDEVTEE
     QVKNAIKTFA NTQGFIIAPE SGHAVATAIK YAREHKDEKK TLLINVSGHG LLDLSIFSD