TRPB_CLOBB
ID TRPB_CLOBB Reviewed; 405 AA.
AC B2TM49;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=CLL_A1973;
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001056; ACD23594.1; -; Genomic_DNA.
DR RefSeq; WP_012424400.1; NC_018648.1.
DR AlphaFoldDB; B2TM49; -.
DR SMR; B2TM49; -.
DR EnsemblBacteria; ACD23594; ACD23594; CLL_A1973.
DR KEGG; cbk:CLL_A1973; -.
DR PATRIC; fig|935198.13.peg.1925; -.
DR HOGENOM; CLU_016734_3_1_9; -.
DR OMA; GPEHAMF; -.
DR OrthoDB; 912282at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001195; 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..405
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000095783"
FT MOD_RES 96
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 405 AA; 44770 MW; 61EC889542759B7B CRC64;
MDFRTYLKKY PDKNGRFGQY GGAYLTAELI PAFEEIADAY QTICHSSQFI NELRRIRKEF
QGRPTPVYHC ERLSRAIGNC QIYLKREDLN HTGAHKLNHC MGEGLLAKFM GKKRLIAETG
AGQHGVALAT AAAFFGLECE IHMGEVDIAK QAPNVTRMKI LGAKVVPVTH GLKTLKEAVD
SAFDSYAKNY KDSIYCIGSA LGPHPFPLMV RDFQAVVGYE AKDQFKEMTG FLPDVVTACV
GGGSNAAGMF IPFLEEPVDI IGIEPLGRGE KLGDHAASMK YGEKGVMHGF ESIMLKDKNG
DPAPVYSIAS GLDYPSVGPE HAFLRELGRV DYKVINDEEA MEAFFKLSRY EGIIPAIESS
HAVAYAMKKA EEMKQGSILV CLSGRGDKDI DYIVEHYGYG EQYFK
