(data stored in ACNUC7421 zone)

SWISSPROT: TRPB_RHOPS

ID   TRPB_RHOPS              Reviewed;         404 AA.
AC   Q13EQ2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   11-DEC-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}; OrderedLocusNames=RPD_0197;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-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}.
DR   EMBL; CP000283; ABE37437.1; -; Genomic_DNA.
DR   RefSeq; WP_011500629.1; NC_007958.1.
DR   SMR; Q13EQ2; -.
DR   STRING; 316057.RPD_0197; -.
DR   EnsemblBacteria; ABE37437; ABE37437; RPD_0197.
DR   KEGG; rpd:RPD_0197; -.
DR   eggNOG; ENOG4105CG0; Bacteria.
DR   eggNOG; COG0133; LUCA.
DR   HOGENOM; HOG000161710; -.
DR   KO; K01696; -.
DR   OMA; PEMLYPN; -.
DR   OrthoDB; 912282at2; -.
DR   BioCyc; RPAL316057:RPD_RS01000-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001818; 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   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; Q13EQ2.
DR   SWISS-2DPAGE; Q13EQ2.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Pyridoxal phosphate; Tryptophan biosynthesis.
FT   CHAIN           1..404
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_1000095813"
FT   MOD_RES         98
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   404 AA;  43820 MW;  3BBB526D1D2A41A1 CRC64;
     MNQILPNSFR SGPDERGHFG IFGGRFVAET LMPLILELEK AYAEAKDDPA FRTEMDGYLK
     HYVGRPSPLY FAERLTEHFG GAKIYFKRED LNHTGAHKVN NVLGQIMLAR RMGKQRIIAE
     TGAGMHGVAT ATMCAKFGLQ CVVYMGAVDV ERQQPNVLRM KALGAEVRPV TSGANTLKDA
     MNEALRDWVT NVHDTFYCIG TVAGPHPYPM MVRDFQEVIG QEVREQILET EGRLPDSLIA
     CIGGGSNAMG LFHPFLDDAG VVIYGVEAAG HGLSKLHAAS IAGGKPGVLH GNRTYLLMDD
     DGQIQEAHSI SAGLDYPGIG PEHAWLHDVG RVNFLSATDA EALDAFKLCC RLEGIIPALE
     PAHALAKVAD LAPILPKDHL MVLNMSGRGD KDLASVAEHL GGKF
//

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