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Database: UniProt/TrEMBL
Entry: D5X4K8_THIK1
LinkDB: D5X4K8_THIK1
Original site: D5X4K8_THIK1 
ID   D5X4K8_THIK1            Unreviewed;       292 AA.
AC   D5X4K8;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   11-JUN-2014, entry version 25.
DE   RecName: Full=Tryptophan synthase alpha chain;
DE            EC=4.2.1.20;
GN   Name=trpA; OrderedLocusNames=Tint_2323;
OS   Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Thiomonas.
OX   NCBI_TaxID=75379;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA   Heinhorst S., Woyke T.;
RT   "Complete sequence of Thiomonas intermedia K12.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage
CC       of indoleglycerol phosphate to indole and glyceraldehyde 3-
CC       phosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3-
CC       phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O.
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 TrpA family.
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DR   EMBL; CP002021; ADG31672.1; -; Genomic_DNA.
DR   RefSeq; YP_003644002.1; NC_014153.1.
DR   ProteinModelPortal; D5X4K8; -.
DR   EnsemblBacteria; ADG31672; ADG31672; Tint_2323.
DR   GeneID; 9153057; -.
DR   KEGG; tin:Tint_2323; -.
DR   PATRIC; 38295189; VBIThiInt85915_2340.
DR   HOGENOM; HOG000223815; -.
DR   KO; K01695; -.
DR   BioCyc; TINT75379:GH6C-2358-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00131; Trp_synth_alpha; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR018204; Trp_synthase_alpha_AS.
DR   InterPro; IPR002028; Trp_synthase_suA.
DR   Pfam; PF00290; Trp_syntA; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR00262; trpA; 1.
DR   PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Tryptophan biosynthesis.
FT   ACT_SITE     76     76       Proton acceptor (By similarity){EA5}.
FT   ACT_SITE     87     87       Proton acceptor (By similarity){EA5}.
SQ   SEQUENCE   292 AA;  30688 MW;  1F5667CB59E6E6D1 CRC64;
     MKQPPDSLRS SPPEGVSVPS GRPRGTDMNR IDQRFAQLRA QNRKALIPYI AAGDPAPSVT
     VEVMHALVQG GADVIELGVP FSDPMADGPV IQRATERAIT KGIGLPQVLD FVRDFRQTDA
     VTPVVLMGYA NPVERYGVEA FVAAAKAAGV DGVLIVDYPP AESEAFAAAL KAADIAPIFL
     LAPTSTDARM ADVGRIASGY VYYVSLKGVT GAGHLDTSAV AAMLPRIRAH VQVPVGVGFG
     IRDAQTARAI GQLADAVVIG SRLIELMEAQ PAEQAAEVAR GFIQDIRQAL DA
//
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