(data stored in SCRATCH zone)

HOGENOM: STACT_1_PE1009

ID   STACT_1_PE1009                       STANDARD;      PRT;   409 AA.
AC   STACT_1_PE1009; B9DP39;
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   (STACT_1.PE1009).
GN   Name=trpB; OrderedLocusNames=Sca_1017; ORFNames=SCA_1017;
OS   STAPHYLOCOCCUS CARNOSUS SUBSP. CARNOSUS TM300.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=396513;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STACT_1.PE1009.
CC       Staphylococcus carnosus subsp. carnosus TM300, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:B9DP39_STACT
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; B9DP39; -.
DR   EMBL; AM295250; CAL27925.1; -; Genomic_DNA.
DR   RefSeq; YP_002634110.1; NC_012121.1.
DR   STRING; B9DP39; -.
DR   EnsemblBacteria; EBSTAT00000051747; EBSTAP00000048999; EBSTAG00000050066.
DR   GeneID; 7552265; -.
DR   GenomeReviews; AM295250_GR; Sca_1017.
DR   KEGG; sca:Sca_1017; -.
DR   GeneTree; EBGT00050000024423; -.
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:HAMAP.
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; STACT_1.PE1009; -.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Pyridoxal phosphate;
KW   Tryptophan biosynthesis.
SQ   SEQUENCE   409 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTKDTKQPIQ TEVDELGFFG EYGGRYVPET LMPAIQELRQ AYEEAKDDPA FQEELAGYLK
     DYVGRATPLT YADSYTKQLG GAKIYLKRED LNHTGAHKIN NALGQALLAK RMGKKKLVAE
     TGAGQHGVAS ATVAALFDME LVVFMGEEDI QRQALNVFRM ELLGAKVVSV TDGQGTLSDA
     VNKALQYWVS HVEDTHYLLG SALGPDPFPT MVRDFQSVIG SEIKEQLQEK EGRLPDAVVA
     CVGGGSNSIG TFYPFVEDES VKLYGVEAAG DGEDTDKHAL AIGKGSVGVL HGTKMYLLQN
     EEGQIGLAHS ISAGLDYPGI GPEHSYYSDI GRAEYPSASD DEAMEALVRF TKAEGIIPAI
     ESAHALSYVE KLAPTMDKDE IIVVTVSGRG DKDMDTIRKY MKERGADNE
//

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