ID   TRPB_METLZ              Reviewed;         392 AA.
AC   A2STA4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=Mlab_1394;
OS   Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX   NCBI_TaxID=410358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43576 / DSM 4855 / Z;
RX   PubMed=21304657; DOI=10.4056/sigs.35575;
RA   Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL   Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN07560.1; -; Genomic_DNA.
DR   RefSeq; WP_011833763.1; NC_008942.1.
DR   AlphaFoldDB; A2STA4; -.
DR   SMR; A2STA4; -.
DR   STRING; 410358.Mlab_1394; -.
DR   EnsemblBacteria; ABN07560; ABN07560; Mlab_1394.
DR   GeneID; 4795847; -.
DR   KEGG; mla:Mlab_1394; -.
DR   eggNOG; arCOG01433; Archaea.
DR   HOGENOM; CLU_016734_3_1_2; -.
DR   OMA; HGMKSYF; -.
DR   OrthoDB; 24741at2157; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000365; 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..392
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_1000117760"
FT   MOD_RES         86
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   392 AA;  42651 MW;  F5F2B3D66A0761D6 CRC64;
     MKEKTGYYGE FGGRFVPETL MAALYELDSA YHRLKDDPGF KAELNSYLTE FAGRETPLTF
     CRNMSEYCGC KVYLKREDLV HGGAHKLNNT LGQALLAKAM GKKRLIAETG AGQHGVATAI
     AGAALNLPVE VFMGEEDCER QKLNVFRMEL MGAKVHPVSS GTKTLKDATN EALREWAKTV
     DYTHYLIGSV VGPHPFPMIV RDFQSVIGEE TRRQCLEKEG RLPDTLVACV GGGSNAIGMF
     YPMLNDDVRM VGVEAGGRAL TPGNNGATLN TGSPGILHGA LSYLIQNDDG QVGVTHSISA
     GLDYPGVGPE HSMLKDLNRV EYSYVMDDEV LEAFSYLSRT EGIIPALESA HAVSYVLKNR
     DSFDRDDIVV ICLSGRGDKD VSSVSKMFGG EE