(data stored in ACNUC7421 zone)

SWISSPROT: Q13S25_PARXL

ID   Q13S25_PARXL            Unreviewed;       397 AA.
AC   Q13S25;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 100.
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   ORFNames=Bxe_B2881 {ECO:0000313|EMBL:ABE33114.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33114.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33114.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33114.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000271; ABE33114.1; -; Genomic_DNA.
DR   RefSeq; WP_011490497.1; NZ_CP008762.1.
DR   STRING; 266265.Bxe_B2881; -.
DR   EnsemblBacteria; ABE33114; ABE33114; Bxe_B2881.
DR   GeneID; 4006754; -.
DR   KEGG; bxb:DR64_5211; -.
DR   KEGG; bxe:Bxe_B2881; -.
DR   PATRIC; fig|266265.5.peg.4808; -.
DR   eggNOG; ENOG4105CG0; Bacteria.
DR   eggNOG; COG0133; LUCA.
DR   HOGENOM; HOG000161710; -.
DR   KO; K01696; -.
DR   OMA; HGMKSYF; -.
DR   OrthoDB; 912282at2; -.
DR   BioCyc; BXEN266265:BXE_RS22790-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001817; 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; Q13S25.
DR   SWISS-2DPAGE; Q13S25.
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};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00015853,
KW   ECO:0000313|EMBL:ABE33114.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015971};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015947}.
FT   DOMAIN       56    380       PALP. {ECO:0000259|Pfam:PF00291}.
FT   MOD_RES      90     90       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00133}.
SQ   SEQUENCE   397 AA;  43350 MW;  9E8D70C470B63F69 CRC64;
     MYNLPDERGH FGQFGGTFVA ETLVHALDEL RAAYGKYQKD PDFVAEYERE LKYFVGRPSP
     IYHAQRWSDM LGGAQIFLKR EDLNHTGAHK INNVIGQALL AKRMGKPRVI AETGAGQHGV
     ATATIAARFG MECVVYMGAE DVRRQAANVY RMKLLGATVV PVESGSRTLK DALNEAMRDW
     VTNVEDTFYI IGTVAGPHPY PMMVRDFQRV IGDECKVQMP ELVGRQPDAV IACVGGGSNA
     MGIFYPYIDD ASVKLIGVEA AGDGIETGRH AASLIGGSPG VLHGNRTYLL QDENGQIIET
     HSVSAGLDYP GVGPEHAWLK ESKRAEYVGI TDEEALKAFH DCCRIEGIIP ALESSHALAY
     ATKLAPTLPK DKYLLVNLSG RGDKDMHTVA ERSGIQF
//

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