TRPB_PSEPW
ID TRPB_PSEPW Reviewed; 405 AA.
AC B1J4B1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=PputW619_0101;
OS Pseudomonas putida (strain W619).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W619;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas putida W619.";
RL Submitted (FEB-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; CP000949; ACA70607.1; -; Genomic_DNA.
DR RefSeq; WP_012312053.1; NC_010501.1.
DR AlphaFoldDB; B1J4B1; -.
DR SMR; B1J4B1; -.
DR STRING; 390235.PputW619_0101; -.
DR EnsemblBacteria; ACA70607; ACA70607; PputW619_0101.
DR KEGG; ppw:PputW619_0101; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_6; -.
DR OMA; GPEHAMF; -.
DR OrthoDB; 912282at2; -.
DR UniPathway; UPA00035; UER00044.
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_1000095804"
FT MOD_RES 95
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 405 AA; 43984 MW; CD457525B4E6CBC1 CRC64;
MTQSQYRPGP DANGLFGSFG GRYVAETLMP LVLDLAREYE AAKADPKFLE ELAYFQRDYI
GRPNPLYFAE RLTEHCGGAK IFFKREELNH TGAHKVNNCI GQVLLAKRMG KKRLIAETGA
GMHGVATATV AARFGLPCVI YMGATDIERQ QANVFRMKLL GAEIVPVTAG TGTLKDAMNE
ALRDWVTNVD DTFYLIGTVA GPHPYPAMVR DFQSIIGKET RAQLQEKEGR LPDSLIACVG
GGSNAMGLFH EFLEDESVKI IGVEAGGHGV NTGKHAASLN GGVPGVLHGN RTYLLQDDDG
QITDAHSISA GLDYPGIGPE HAYLHEVKRV EYVSITDDEA LDAFHATCRL EGIIPALETS
HALAEAIKRA PNLPKDHLMV ICLSGRGDKD MQTVMNHMAA QEKQA