ID   TRPB_MYCLE              Reviewed;         417 AA.
AC   Q9CC54;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=ML1272;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; AL583921; CAC31653.1; -; Genomic_DNA.
DR   PIR; B87068; B87068.
DR   RefSeq; NP_301917.1; NC_002677.1.
DR   RefSeq; WP_010908238.1; NC_002677.1.
DR   AlphaFoldDB; Q9CC54; -.
DR   SMR; Q9CC54; -.
DR   STRING; 272631.ML1272; -.
DR   EnsemblBacteria; CAC31653; CAC31653; CAC31653.
DR   KEGG; mle:ML1272; -.
DR   PATRIC; fig|272631.5.peg.2336; -.
DR   Leproma; ML1272; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_11; -.
DR   OMA; HGMKSYF; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000806; 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; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..417
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098968"
FT   MOD_RES         108
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   417 AA;  44502 MW;  D45B6103B731E63A CRC64;
     MMPNLSCFSV AISEPTCHDP DSGGHFGGPD GYGGRYVPEA LMAVIEEVTA AYEKERVNQD
     FLDLLDKLQA NYAGRPSPLY EATRLSEYAG SVRIFLKRED LNHTGSHKIN NVLGQTLLAQ
     RMGKTRVIAE TGAGQHGVAT ATACALFGLD CVIYMGALDT ARQALNVARM RLLGAEVVSV
     ETGSRTLKDA INDAFRDWVT NADNTYYCFG TASGPHPFPT MVRDLQRVIG LETRRQIQYQ
     AGRLPDAVTA CIGGGSNAIG IFHAFLDDPG VRLVGFEAAG DGVETGRHAA TLTGGLPGAF
     QGTFSYLLQD EDGQTIESHS IAAGLDYPGV GPEHAWLRET GRAEYQPITD SEAIEAFRLL
     CRTEGILPAL ESAHAVAGAL KLASEIGKGA VIVVNLSGRG DKDIEAAAKW FGLLGTR