ID   TRPB2_METTM             Reviewed;         390 AA.
AC   P26921; D9PUE9;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Tryptophan synthase beta chain 2;
DE            EC=4.2.1.20;
GN   Name=trpB2; Synonyms=trpB; OrderedLocusNames=MTBMA_c02380;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=1860817; DOI=10.1128/jb.173.16.5017-5023.1991;
RA   Meile L., Stettler R., Banholzer R., Kotik M., Leisinger T.;
RT   "Tryptophan gene cluster of Methanobacterium thermoautotrophicum Marburg:
RT   molecular cloning and nucleotide sequence of a putative trpEGCFBAD
RT   operon.";
RL   J. Bacteriol. 173:5017-5023(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
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=ADL57847.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; M65060; AAA73032.1; -; Genomic_DNA.
DR   EMBL; CP001710; ADL57847.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P26921; -.
DR   SMR; P26921; -.
DR   STRING; 79929.MTBMA_c02380; -.
DR   EnsemblBacteria; ADL57847; ADL57847; MTBMA_c02380.
DR   KEGG; mmg:MTBMA_c02380; -.
DR   PATRIC; fig|79929.8.peg.234; -.
DR   HOGENOM; CLU_016734_3_1_2; -.
DR   OMA; HGMKSYF; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000345; 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; Tryptophan biosynthesis.
FT   CHAIN           1..390
FT                   /note="Tryptophan synthase beta chain 2"
FT                   /id="PRO_0000099044"
FT   MOD_RES         83
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   390 AA;  42116 MW;  ECA164EB4B35B8DF CRC64;
     MDGKFGKYGG IFVPELLIPA LEELEAAFLH YSKDRRFNED LEHYLREYAG RPTGLYHARN
     LSEKLGCRVY LKREDMLHTG AHKINNTIGQ ALLAGYMGKR RLIAETGAGQ HGIATAAAGA
     LFGMDVDVYM GTEDVERQKL NVFRMEISGA RVIPVDSGSR TLKDAINQAM RDWISSVEDT
     HYLIGSTMGP HPYPTMVKHF QSVIGREARE QILEIEGELP DTIIACVGGG SNAIGIFSAF
     LDDDVELIGA EGGGEGIESG NHGATLSAGS EGVLHGSLSY VLQDDDGQIN EAHSVSAGLD
     YPGVGPEHAY LMETGRAMYE PITDAEALRG FKLLSRCEGI MPALESAHAI ACLEKYASKP
     ENRGKTVIVN LSGRGDKDMF LAAGLLGVDL