ID   TRPB_BACSU              Reviewed;         400 AA.
AC   P07600;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=BSU22640;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3924737; DOI=10.1016/0378-1119(85)90125-8;
RA   Henner D.J., Band L., Shimotsu H.;
RT   "Nucleotide sequence of the Bacillus subtilis tryptophan operon.";
RL   Gene 34:169-177(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 122 AND 398.
RX   PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA   Medigue C., Rose M., Viari A., Danchin A.;
RT   "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT   the Bacillus subtilis genome sequence.";
RL   Genome Res. 9:1116-1127(1999).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine.
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; M80245; AAA20865.1; -; Genomic_DNA.
DR   EMBL; K01391; AAA22869.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14180.2; -; Genomic_DNA.
DR   PIR; E22794; E22794.
DR   RefSeq; NP_390145.2; NC_000964.3.
DR   RefSeq; WP_003230605.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P07600; -.
DR   SMR; P07600; -.
DR   STRING; 224308.BSU22640; -.
DR   PaxDb; P07600; -.
DR   PRIDE; P07600; -.
DR   EnsemblBacteria; CAB14180; CAB14180; BSU_22640.
DR   GeneID; 939010; -.
DR   KEGG; bsu:BSU22640; -.
DR   eggNOG; COG0133; Bacteria.
DR   InParanoid; P07600; -.
DR   OMA; HGMKSYF; -.
DR   PhylomeDB; P07600; -.
DR   BioCyc; BSUB:BSU22640-MON; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001570; 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..400
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098918"
FT   MOD_RES         90
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        122
FT                   /note="A -> P (in Ref. 1; AAA20865/AAA22869)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398
FT                   /note="A -> R (in Ref. 1; AAA20865/AAA22869)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   400 AA;  43580 MW;  B875A9A9970962AD CRC64;
     MYPYPNEIGR YGDFGGKFVP ETLMQPLDEI QTAFKQIKDD PAFREEYYKL LKDYSGRPTA
     LTYADRVTEY LGGAKIYLKR EDLNHTGSHK INNALGQALL AKKMGKTKII AETGAGQHGV
     AAATVAAKFG FSCTVFMGEE DVARQSLNVF RMKLLGAEVV PVTSGNGTLK DATNEAIRYW
     VQHCEDHFYM IGSVVGPHPY PQVVREFQKM IGEEAKDQLK RIEGTMPDKV VACVGGGSNA
     MGMFQAFLNE DVELIGAEAA GKGIDTPLHA ATISKGTVGV IHGSLTYLIQ DEFGQIIEPY
     SISAGLDYPG IGPEHAYLHK SGRVTYDSIT DEEAVDALKL LSEKEGILPA IESAHALAKA
     FKLAKGMDRG QLILVCLSGR GDKDVNTLMN VLEEEVKAHV