ID   TRPB_PSEAE              Reviewed;         402 AA.
AC   P07345;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=PA0036;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=3127651; DOI=10.1093/oxfordjournals.molbev.a040388;
RA   Hadero A., Crawford I.P.;
RT   "Nucleotide sequence of the genes for tryptophan synthase in Pseudomonas
RT   aeruginosa.";
RL   Mol. Biol. Evol. 3:191-204(1986).
RN   [2]
RP   SEQUENCE REVISION.
RA   Crawford I.P.;
RL   Submitted (MAY-1987) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; M15826; AAA88462.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG03426.1; -; Genomic_DNA.
DR   PIR; A25355; TSPSBA.
DR   PIR; H83640; H83640.
DR   RefSeq; NP_248726.1; NC_002516.2.
DR   RefSeq; WP_003097340.1; NZ_QZGE01000012.1.
DR   AlphaFoldDB; P07345; -.
DR   SMR; P07345; -.
DR   STRING; 287.DR97_2990; -.
DR   PaxDb; P07345; -.
DR   PRIDE; P07345; -.
DR   DNASU; 879212; -.
DR   EnsemblBacteria; AAG03426; AAG03426; PA0036.
DR   GeneID; 879212; -.
DR   KEGG; pae:PA0036; -.
DR   PATRIC; fig|208964.12.peg.36; -.
DR   PseudoCAP; PA0036; -.
DR   HOGENOM; CLU_016734_3_1_6; -.
DR   InParanoid; P07345; -.
DR   OMA; GPEHAMF; -.
DR   PhylomeDB; P07345; -.
DR   BioCyc; PAER208964:G1FZ6-37-MON; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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..402
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098981"
FT   MOD_RES         93
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        16
FT                   /note="R -> G (in Ref. 1; AAA88462)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="V -> L (in Ref. 1; AAA88462)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        325
FT                   /note="T -> I (in Ref. 1; AAA88462)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   402 AA;  43681 MW;  F4D59601BBDFC016 CRC64;
     MTSYRNGPDA KGLFGRFGGQ YVAETLMPLI LDLAREYEKA KDDPAFQEEL AYFQRDYVGR
     PSPLYFAERL TEHCGGAKIY LKREELNHTG AHKINNCIGQ ILLARRMGKK RIIAETGAGM
     HGVATATVAA RFGLQCVIYM GTTDIDRQQA NVFRMKLLGA EVIPVTAGTG TLKDAMNEAL
     RDWVTNVDST FYLIGTVAGP HPYPAMVRDF QAVIGKETRE QLAEKEGRLP DSLVACIGGG
     SNAMGLFHPF LDDAGVQIVG VEAAGHGIDT GKHAASLNGG VPGVLHGNRT FLLQDADGQI
     IDAHSISAGL DYPGIGPEHA WLHDTGRVEY TSITDDEALE AFHTCCRLEG IIPALESSHA
     LAEVFKRAPS LPKEHIMVVN LSGRGDKDMQ TVMHHMQQES KA