ID   TRPB1_METMA             Reviewed;         403 AA.
AC   Q8PT95;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 2.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Tryptophan synthase beta chain 1;
DE            EC=4.2.1.20;
GN   Name=trpB1; OrderedLocusNames=MM_2822;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM32518.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008384; AAM32518.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011034730.1; NC_003901.1.
DR   AlphaFoldDB; Q8PT95; -.
DR   SMR; Q8PT95; -.
DR   STRING; 192952.MM_2822; -.
DR   EnsemblBacteria; AAM32518; AAM32518; MM_2822.
DR   GeneID; 24878180; -.
DR   GeneID; 66135217; -.
DR   KEGG; mma:MM_2822; -.
DR   PATRIC; fig|192952.21.peg.3257; -.
DR   eggNOG; arCOG01433; Archaea.
DR   HOGENOM; CLU_016734_3_1_2; -.
DR   OMA; HGMKSYF; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000595; Chromosome.
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; 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..403
FT                   /note="Tryptophan synthase beta chain 1"
FT                   /id="PRO_0000099040"
FT   MOD_RES         93
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   403 AA;  43753 MW;  B698C24E17689701 CRC64;
     MAAAIISELQ VKGKYGKYGG QYVPEVLMPA LEELEEGYER YKNDPEFLAE LDHYLRDFAG
     RETPLYLARN LSKKYGTKIY LKREDLVHGG AHKLNNAIGQ ALLAKYMGKT RLIAETGAGQ
     HGTATAMAGA NLGFETVVYM GAKDVKRQQM NAYRMELMGT EVKPVKTGSK TLKDAINEAF
     RDWVTNIGNT HYLIGSVVGP HPYPMIVRDF QSVIGREVKE QAMEKEGRLP DTIIACAGGG
     SNAMGTFYPF IEDRDVRLIA VEAGGKALRC TEKAALHSAS LCAGEEGILH GARTKVLQDK
     NGQILESESV SAGLDYSGVG PELASLAESG RVTARYVTDD EAVEAFNELS RLEGIIPALE
     SSHALAYLKK AAESGELGEF VVVNLSGRGD KDLETVLSLK RGI