ID   TRPB_MYCTO              Reviewed;         421 AA.
AC   P9WFX8; L0T779; O08376; P66984;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 2.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=MT1647;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45916.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000250|UniProtKB:P9WFX9};
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DR   EMBL; AE000516; AAK45916.1; ALT_INIT; Genomic_DNA.
DR   PIR; B70557; B70557.
DR   AlphaFoldDB; P9WFX8; -.
DR   SMR; P9WFX8; -.
DR   EnsemblBacteria; AAK45916; AAK45916; MT1647.
DR   KEGG; mtc:MT1647; -.
DR   HOGENOM; CLU_016734_3_1_11; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001020; 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..421
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000428459"
FT   MOD_RES         112
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   421 AA;  44514 MW;  FB00A3153CA8F7BC CRC64;
     MTDLSTPDLP RMSAAIAEPT SHDPDSGGHF GGPSGWGGRY VPEALMAVIE EVTAAYQKER
     VSQDFLDDLD RLQANYAGRP SPLYEATRLS QHAGSARIFL KREDLNHTGS HKINNVLGQA
     LLARRMGKTR VIAETGAGQH GVATATACAL LGLDCVIYMG GIDTARQALN VARMRLLGAE
     VVAVQTGSKT LKDAINEAFR DWVANADNTY YCFGTAAGPH PFPTMVRDFQ RIIGMEARVQ
     IQGQAGRLPD AVVACVGGGS NAIGIFHAFL DDPGVRLVGF EAAGDGVETG RHAATFTAGS
     PGAFHGSFSY LLQDEDGQTI ESHSISAGLD YPGVGPEHAW LKEAGRVDYR PITDSEAMDA
     FGLLCRMEGI IPAIESAHAV AGALKLGVEL GRGAVIVVNL SGRGDKDVET AAKWFGLLGN
     D