ID   TRPB_STRCO              Reviewed;         427 AA.
AC   O05625;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   25-MAY-2022, entry version 140.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=SCO2037; ORFNames=SC4G6.06c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=10361288; DOI=10.1046/j.1365-2958.1999.01407.x;
RA   Hu D.S.-J., Hood D.W., Heidstra R., Hodgson D.A.;
RT   "The expression of the trpD, trpC and trpBA genes of Streptomyces
RT   coelicolor A3(2) is regulated by growth rate and growth phase but not by
RT   feedback repression.";
RL   Mol. Microbiol. 32:869-880(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 320-427.
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=9097426; DOI=10.1128/aem.63.4.1288-1297.1997;
RA   Huddleston A.S., Cresswell N., Neves M.C., Beringer J.E., Baumberg S.,
RA   Thomas D.I., Wellington E.M.;
RT   "Molecular detection of streptomycin-producing streptomycetes in Brazilian
RT   soils.";
RL   Appl. Environ. Microbiol. 63:1288-1297(1997).
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; AF054585; AAC63502.1; -; Genomic_DNA.
DR   EMBL; AL939111; CAB51429.1; -; Genomic_DNA.
DR   EMBL; U72185; AAB52397.1; -; Genomic_DNA.
DR   PIR; T35066; T35066.
DR   RefSeq; NP_626297.1; NC_003888.3.
DR   RefSeq; WP_003976779.1; NZ_VNID01000001.1.
DR   AlphaFoldDB; O05625; -.
DR   SMR; O05625; -.
DR   STRING; 100226.SCO2037; -.
DR   GeneID; 1097471; -.
DR   KEGG; sco:SCO2037; -.
DR   PATRIC; fig|100226.15.peg.2068; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_11; -.
DR   InParanoid; O05625; -.
DR   OMA; HGMKSYF; -.
DR   PhylomeDB; O05625; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; 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..427
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000099006"
FT   MOD_RES         100
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   427 AA;  45384 MW;  9CB87BEDA3851F9A CRC64;
     MPSNFFIPDP EGQVPSAEGY FGAFGGKFIP EALVAAVDEV AVEYDKAKSD PEFARELDDL
     LVHYTGRPSA LTEVPRFAAE AGGARIFLKR EDLNHTGSHK INNVLGQALL TKRMGKTRVI
     AETGAGQHGV ATATACALFG LDCTIYMGEI DTRRQALNVA RMRMLGAEVI AVKSGSRTLK
     DAINEAFRDW VANVDRTHYL FGTVAGPHPF PAMVRDFHRV IGVEARRQLL EQAGRLPDAA
     IACVGGGSNA IGLFHAFIPD ADVRLIGCEP AGHGVETGEH AATLTAGEPG ILHGSRSYVL
     QDDEGQITEP YSISAGLDYP GIGPEHAYLK DSGRGEYRAV TDDAAMQALR LLSRTEGIIP
     AIESAHALAG ALEVGRELGR DGLLVVNLSG RGDKDMDTAA RYFGLYDTDA EVAADGTGAA
     EIEGDAK