(data stored in ACNUC7421 zone)

SWISSPROT: TRPB_PSEU2

ID   TRPB_PSEU2              Reviewed;         409 AA.
AC   Q500R4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 87.
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=Psyr_0034;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine =
CC         D-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;
CC         EC=4.2.1.20; 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00133}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
DR   EMBL; CP000075; AAY35108.1; -; Genomic_DNA.
DR   RefSeq; WP_003401519.1; NC_007005.1.
DR   RefSeq; YP_233146.1; NC_007005.1.
DR   SMR; Q500R4; -.
DR   STRING; 205918.Psyr_0034; -.
DR   PRIDE; Q500R4; -.
DR   EnsemblBacteria; AAY35108; AAY35108; Psyr_0034.
DR   GeneID; 3365509; -.
DR   KEGG; psb:Psyr_0034; -.
DR   PATRIC; fig|205918.7.peg.33; -.
DR   eggNOG; ENOG4105CG0; Bacteria.
DR   eggNOG; COG0133; LUCA.
DR   HOGENOM; HOG000161710; -.
DR   KO; K01696; -.
DR   OMA; GPEHAMF; -.
DR   BioCyc; PSYR205918:G1G4J-34-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd06446; Trp-synth_B; 1.
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   PANTHER; PTHR42882; PTHR42882; 1.
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;
DR   PRODOM; Q500R4.
DR   SWISS-2DPAGE; Q500R4.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Pyridoxal phosphate;
KW   Tryptophan biosynthesis.
FT   CHAIN         1    409       Tryptophan synthase beta chain.
FT                                /FTId=PRO_1000018379.
FT   MOD_RES      95     95       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00133}.
SQ   SEQUENCE   409 AA;  44452 MW;  D6B7755F530D7E4B CRC64;
     MTQTNFRSGP DANGLFGSFG GRYVAETLMP LVLDLNREYE AAKADPEFIK EMAYFQRDYV
     GRPNPLYFAE RLTEFCGGAK IYFKREELNH TGAHKINNCI GQVLLAKRMG KKRLIAETGA
     GMHGVATATV AARFGLPCVI YMGATDIERQ QANVFRMRLL GAEIVPVTSG TGTLKDAMNE
     ALRDWVTNVD DTFYLIGTVA GPHPYPAMVR DFQAIIGKET KEQMLEKEGR LPDSLVACVG
     GGSNAMGLFH PFLDDASVEI IGVEAGGHGV STDKHAASLN GGVPGVLHGN RTYLLQDGDG
     QITDAHSISA GLDYPGIGPE HAFLHEVKRV EYVSITDDEA LDAFHQCCLL EGIIPALETA
     HALAEAMKRA TNLRDDHLMV VCLSGRGDKD MQTVMNHMAA AEHTQEQLV
//

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