ID   TRPB_CLAMS              Reviewed;         404 AA.
AC   B0REU1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Tryptophan synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00133};
DE            EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00133};
GN   Name=trpB {ECO:0000255|HAMAP-Rule:MF_00133}; OrderedLocusNames=CMS2009;
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS   / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX   PubMed=18192393; DOI=10.1128/jb.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000255|HAMAP-Rule:MF_00133}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
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DR   EMBL; AM849034; CAQ02106.1; -; Genomic_DNA.
DR   RefSeq; WP_012299335.1; NZ_MZMN01000003.1.
DR   AlphaFoldDB; B0REU1; -.
DR   SMR; B0REU1; -.
DR   STRING; 31964.CMS2009; -.
DR   EnsemblBacteria; CAQ02106; CAQ02106; CMS2009.
DR   KEGG; cms:CMS2009; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_11; -.
DR   OMA; GPEHAMF; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001318; 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..404
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_1000203191"
FT   MOD_RES         91
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   404 AA;  43071 MW;  2E76A8DC640B65FB CRC64;
     MTDLRSVTGP YFGEFGGRYV PESLVAALDE LSAAWEELKV DPAFVEELKE LHRTYTGRPS
     LITEVPRFAE HAGGARIILK REDLNHTGSH KINNVLGQAL LTKKIGKKRI IAETGAGQHG
     VATATAAALF GLDCVIYMGE VDTERQALNV ARMRLLGAEV IPVRSGSRTL KDAINDAMRD
     WVTNVETTNY VFGTVAGPHP FPAMVRDLQK VIGEEAREQV LALTGRLPDA VAACVGGGSN
     AIGIFHAFLD DADVALYGFE AGGDGADTPR TAATITKGRP GMLHGARSYL LQDEDGQTID
     SHSISAGLDY PGVGPEHSWL SDLGRASYRP VTDDQAMSAL RLLSRTEGII PAIESAHALA
     GALELGKELG PDAIILINLS GRGDKDMETA GKYFDLIDAG AEQS