(data stored in ACNUC1104 zone)

SWISSPROT: B1K368_BURCC

ID   B1K368_BURCC            Unreviewed;       397 AA.
AC   B1K368;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=Tryptophan synthase beta chain {ECO:0000256|HAMAP-Rule:MF_00133};
DE            EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00133};
GN   Name=trpB {ECO:0000256|HAMAP-Rule:MF_00133};
GN   OrderedLocusNames=Bcenmc03_3570 {ECO:0000313|EMBL:ACA92722.1};
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92722.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT   3.";
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:0000256|HAMAP-
CC       Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.
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:0000256|HAMAP-Rule:MF_00133,
CC         ECO:0000256|SAAS:SAAS01118361};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00133,
CC         ECO:0000256|SAAS:SAAS00166768};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00133, ECO:0000256|SAAS:SAAS00015996}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00345877}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00133, ECO:0000256|SAAS:SAAS00541094}.
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DR   EMBL; CP000959; ACA92722.1; -; Genomic_DNA.
DR   RefSeq; WP_011548091.1; NC_010515.1.
DR   EnsemblBacteria; ACA92722; ACA92722; Bcenmc03_3570.
DR   KEGG; bcm:Bcenmc03_3570; -.
DR   HOGENOM; HOG000161710; -.
DR   KO; K01696; -.
DR   OMA; HGMKSYF; -.
DR   BioCyc; BCEN406425:G1GBC-3791-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002169; Chromosome 2.
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; B1K368.
DR   SWISS-2DPAGE; B1K368.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015918};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015879}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002169};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015853};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015971};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015947}.
FT   DOMAIN       56    380       PALP. {ECO:0000259|Pfam:PF00291}.
FT   COILED       20     40       {ECO:0000256|SAM:Coils}.
FT   MOD_RES      90     90       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00133}.
SQ   SEQUENCE   397 AA;  43220 MW;  E45CB529818BBB77 CRC64;
     MYNLPDDRGH FGPYGGVFVA ETLIHALDEL RAAYEKFQND PDFVAEFERE LKYFVGRPSP
     IYHAQRWSEM LGGAQIYLKR EDLNHTGAHK INNVIGQALL AKRMGKKRVI AETGAGQHGV
     ATATICARFG MECVVYMGSE DVRRQAANVY RMKLLGATVV PVESGSRTLK DALNEAMRDW
     VTNIESTFYI IGTVAGPHPY PMMVRDFQRV IGDECKVQMP ELAGRQPDAV IACVGGGSNA
     MGIFYPYIDD TSVQLIGVEA AGDGLDTGHH AASLIAGSPG VLHGNRTYLL QDDNGQIIET
     HSVSAGLDYP GVGPEHAWLK DSGRAQYVPI TDAEALKAFH DCCRIEGIIP ALESSHAIAY
     GVKLAPTLPK DKLLLVNLSG RGDKDMHTVA ERSGIEL
//

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