(data stored in SCRATCH9089 zone)

SWISSPROT: TRPB_PASMU

ID   TRPB_PASMU              Reviewed;         402 AA.
AC   P54203;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   11-DEC-2019, entry version 139.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=PM0578;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15742 / P1059;
RX   PubMed=8581158; DOI=10.1099/13500872-142-1-115;
RA   Jablonski P.E., Jablonski L.M., Pintado O., Sriranganathan N., Hovde C.J.;
RT   "Identification of Pasteurella multocida tryptophan synthase beta-subunit
RT   by antisera against strain P1059.";
RL   Microbiology 142:115-121(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
DR   EMBL; U22344; AAC43609.1; -; Genomic_DNA.
DR   EMBL; AE004439; AAK02662.1; -; Genomic_DNA.
DR   RefSeq; WP_010906736.1; NC_002663.1.
DR   SMR; P54203; -.
DR   PRIDE; P54203; -.
DR   EnsemblBacteria; AAK02662; AAK02662; PM0578.
DR   KEGG; pmu:PM0578; -.
DR   PATRIC; fig|272843.6.peg.585; -.
DR   eggNOG; ENOG4105CG0; Bacteria.
DR   eggNOG; COG0133; LUCA.
DR   HOGENOM; HOG000161710; -.
DR   KO; K01696; -.
DR   OMA; PEMLYPN; -.
DR   BioCyc; PMUL272843:G1FZ8-610-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000809; 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; P54203.
DR   SWISS-2DPAGE; P54203.
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_0000098976"
FT   MOD_RES         88
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        120
FT                   /note="T -> TT (in Ref. 1; AAC43609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        324
FT                   /note="Q -> E (in Ref. 1; AAC43609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        338
FT                   /note="Q -> E (in Ref. 1; AAC43609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="H -> D (in Ref. 1; AAC43609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        366..367
FT                   /note="QP -> HA (in Ref. 1; AAC43609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        399
FT                   /note="Y -> H (in Ref. 1; AAC43609)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   402 AA;  43624 MW;  1F8F38DFD36A2224 CRC64;
     MSETLLNPYF GEFGGMYVPE ILMPVLKNLE KAFVEAQQDP TFKETFLDLL KNYAGRPTAL
     TRCRNLTQGS KTKLYLKRED LLHGGAHKTN QVLGQILLAK RMGKTRIIAE TGAGQHGVAT
     ALACAMLGMP CQIYMGAKDV ERQSPNVFRM RLMGANVTAV TKGSASLKDA CCEAMRDWAE
     NYEHTHYLLG TAAGPHPFPT IVREFQKIIG EETKQQILAR EGRLPDAVIA AVGGGSNAIG
     MFNDFIEETS VRLIGVEPAG KGIATGQHGA PLGHGTTGIY FGMKAPLMQT PDGQIEESYS
     ISAGLDFPSV GPQHAHLQAI GRAQYESITD DEALSAFQAL ARHEGIIPAL ESAHALAYAL
     KLIQRQPEKE QLLVVNLSGR GDKDIFTVDR ILSQKGVSYA PF
//

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