ID   TRPB2_METAC             Reviewed;         442 AA.
AC   Q8TL44;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Tryptophan synthase beta chain 2;
DE            EC=4.2.1.20;
GN   Name=trpB2; OrderedLocusNames=MA_3198;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(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}.
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DR   EMBL; AE010299; AAM06569.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TL44; -.
DR   SMR; Q8TL44; -.
DR   STRING; 188937.MA_3198; -.
DR   EnsemblBacteria; AAM06569; AAM06569; MA_3198.
DR   KEGG; mac:MA_3198; -.
DR   HOGENOM; CLU_042858_1_0_2; -.
DR   InParanoid; Q8TL44; -.
DR   OMA; MLHQTII; -.
DR   PhylomeDB; Q8TL44; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002487; 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_0000099037"
FT   MOD_RES         122
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   442 AA;  49079 MW;  3DB3004C6C16592E CRC64;
     MYRNDVKEIS MEQTKIILDE NEMPKKWYNV LADLPSPIDP PLDPRTWQPI SPDALEPIFP
     KALIMQEMSS DRYIDIPEEV LDVYRLWRPS PLFRAHQLEK VLKSPAKIYY KYEGVSPAGS
     HKTNTSIAQA YYNMKEGTER LTTETGAGQW GSALSLACNY FDLECKVYMV RSSFYQKPYR
     KSLITLWGGN VVPSPSPDTE FGRKILQEQP DTPGSLGIAI SEAVEDAIAH ENTKYSLGSV
     LNHVVLHQTV IGAECKQQLA QVEEYPDVVI GCCGGGSNLG GIGLEFIKDR LEGKHSARVV
     AVEPSACPSL TKGEYRYDFG DTAEMTPLLK MYTLGHKHVP PAIHAGGLRY HGDSPIISKL
     CSEGLMEAVS YDQQEVFDAA VQFARTEGIV PAPESSHAIR CAIDEALAAK QTGEEKTILF
     NLSGHGHFDM SSYDKYFSGE LM