(data stored in SCRATCH zone)

HOGENOM: PSEPW_1_PE101

ID   PSEPW_1_PE101                        STANDARD;      PRT;   405 AA.
AC   PSEPW_1_PE101; B1J4B1;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Tryptophan synthase beta chain; EC=4.2.1 20;
DE   (PSEPW_1.PE101).
GN   Name=trpB; OrderedLocusNames=PputW619_0101;
OS   PSEUDOMONAS PUTIDA W619.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PSEPW_1.PE101.
CC       Pseudomonas putida W619 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:TRPB_PSEPW
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3-
CC       phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
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 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the trpB family.
CC   -!- GENE_FAMILY: HOG000161710 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B1J4B1; -.
DR   EMBL; CP000949; ACA70607.1; -; Genomic_DNA.
DR   RefSeq; YP_001746976.1; NC_010501.1.
DR   ProteinModelPortal; B1J4B1; -.
DR   SMR; B1J4B1; 16-395.
DR   STRING; B1J4B1; -.
DR   GeneID; 6109271; -.
DR   GenomeReviews; CP000949_GR; PputW619_0101.
DR   KEGG; ppw:PputW619_0101; -.
DR   OMA; LKREDLC; -.
DR   ProtClustDB; PRK04346; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:EC.
DR   HAMAP; MF_00133; Trp_synth_beta; 1; -.
DR   InterPro; IPR001926; PyrdxlP-dep_enz_bsu.
DR   InterPro; IPR006653; Trp_synth_b_CS.
DR   InterPro; IPR006654; Trp_synth_beta.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR   SUPFAM; SSF53686; PyrdxlP-dep_enz_bsu; 1.
DR   TIGRFAMs; TIGR00263; TrpB; 1.
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
DR   HOGENOMDNA; PSEPW_1.PE101; -.
KW   tryptophan synthase subunit beta;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Pyridoxal phosphate;
KW   Tryptophan biosynthesis.
SQ   SEQUENCE   405 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTQSQYRPGP DANGLFGSFG GRYVAETLMP LVLDLAREYE AAKADPKFLE ELAYFQRDYI
     GRPNPLYFAE RLTEHCGGAK IFFKREELNH TGAHKVNNCI GQVLLAKRMG KKRLIAETGA
     GMHGVATATV AARFGLPCVI YMGATDIERQ QANVFRMKLL GAEIVPVTAG TGTLKDAMNE
     ALRDWVTNVD DTFYLIGTVA GPHPYPAMVR DFQSIIGKET RAQLQEKEGR LPDSLIACVG
     GGSNAMGLFH EFLEDESVKI IGVEAGGHGV NTGKHAASLN GGVPGVLHGN RTYLLQDDDG
     QITDAHSISA GLDYPGIGPE HAYLHEVKRV EYVSITDDEA LDAFHATCRL EGIIPALETS
     HALAEAIKRA PNLPKDHLMV ICLSGRGDKD MQTVMNHMAA QEKQA
//

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