TRPB_SYNPW
ID TRPB_SYNPW Reviewed; 416 AA.
AC A5GP60;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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};
GN OrderedLocusNames=SynWH7803_2299;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-2006) 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; CT971583; CAK24725.1; -; Genomic_DNA.
DR RefSeq; WP_011934186.1; NC_009481.1.
DR AlphaFoldDB; A5GP60; -.
DR SMR; A5GP60; -.
DR STRING; 32051.SynWH7803_2299; -.
DR EnsemblBacteria; CAK24725; CAK24725; SynWH7803_2299.
DR KEGG; syx:SynWH7803_2299; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_3; -.
DR OMA; HGMKSYF; -.
DR OrthoDB; 912282at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001566; 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..416
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000018413"
FT MOD_RES 109
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 416 AA; 44486 MW; 7DDCD0D85C285FAD CRC64;
MTSTLPSQPS ASDLAVSSRP AAAGRFGRYG GQYVPETLMP ALAELEQAAA QAWKDPAFTA
ELNRLLKSYV GRATPLYEAE RLTEHYRRAD GGPRIWLKRE DLNHTGAHKI NNALGQALLA
LRMGKKRVIA ETGAGQHGVA TATVCARFGL ECVVYMGAED MRRQALNVFR MRLLGATVHP
VTAGTATLKD ATSEAIRDWV TNVETTHYIL GSVAGPHPYP MLVRDFHAVI GQETRQQCRE
AFGRLPDVLM ACVGGGSNAM GLFHPFVECT DVRLIGVEAA GDGVATGRHA ATITEGRVGV
LHGAMSLLLQ DQDGQVQEAH SISAGLDYPG VGPEHSYLRE IGRAEYGAVT DAEALEALQL
VSRLEGIIPA LETAHAFAWL ETLCPTLSAG TEVVLNCSGR GDKDVNTVAE RLGDAL
