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Database: UniProt/TrEMBL
Entry: E8WNR5_GEOS8
LinkDB: E8WNR5_GEOS8
Original site: E8WNR5_GEOS8 
ID   E8WNR5_GEOS8            Unreviewed;       691 AA.
AC   E8WNR5;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   11-JUN-2014, entry version 20.
DE   RecName: Full=Transketolase;
DE            EC=2.2.1.1;
GN   OrderedLocusNames=GM18_1241;
OS   Geobacter sp. (strain M18).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=443143;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M18;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Pagani I., Holmes D., Aklujkar M., Lovley D., Woyke T.;
RT   "Complete sequence of Geobacter sp. M18.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from
CC       a ketose donor to an aldose acceptor, via a covalent intermediate
CC       with the cofactor thiamine pyrophosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit. Can also utilize
CC       other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+)
CC       (By similarity).
CC   -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the transketolase family.
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DR   EMBL; CP002479; ADW12711.1; -; Genomic_DNA.
DR   RefSeq; YP_004197987.1; NC_014973.1.
DR   ProteinModelPortal; E8WNR5; -.
DR   EnsemblBacteria; ADW12711; ADW12711; GM18_1241.
DR   GeneID; 10196834; -.
DR   KEGG; geb:GM18_1241; -.
DR   PATRIC; 46946401; VBIGeoSp68312_1243.
DR   HOGENOM; HOG000225953; -.
DR   KO; K00615; -.
DR   OMA; PMGMAPI; -.
DR   BioCyc; GSP443143:GHZL-1274-MONOMER; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR005478; Transketolase_bac-like.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR005476; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Calcium; Complete proteome; Magnesium; Metal-binding;
KW   Thiamine pyrophosphate; Transferase.
SQ   SEQUENCE   691 AA;  74624 MW;  C3BF423AA673CE9D CRC64;
     MTTLSAMAPA TDLDQLCINT LRFLSVDAVQ KANSGHPGMP MGAAPMAYLL WTRLLKHNPA
     DPGWFDRDRF VLSAGHGSML LYSLLHLTGY DLPLEELRRF RQWGSRTPGH PERGLTPGVE
     VSTGPLGQGF GNAVGMAMAE AHLAARFNRP GYRLIDHYSY LIAGDGDLME GVVSEAASLA
     GHLRLGKLIC LYDDNRITLA ASTALSFSED RAARFSAFGW QVLAVEDGND LEAIGRALEE
     ARADLGRPSL IMVRTRIGFG SPGKQDTFEA HGAPLGAEEV RRSKERLGWP LEPEFHLPER
     ALERFQKARE QGAAAERDWE ELRARYGSEH PELAAELGLA LSGELPEGWQ EALPEFPPDA
     KGMATRAASG KVLNALAGRL PQLFGGSADL NPSTLTALAG KGDFQSETWQ PEDRQGAVGG
     EWGRGGANIH FGVREHGMAA IMNGMAAHGG TIPFGATFLT FSDYLRPALR LAALSDLKVI
     HVFTHDSIAL GEDGPTHQPV EQLASLRAIP RLVVLRPCDA NESAFAWRAA LCVKDRPVAL
     VLSRQAVPTL ERELYAGAEG LLRGGYVLAE AEGGAPQLIL IATGAEVPLA LQARLKLREE
     GLAARVVSLP SWEIFDEQPK EYREEVLPPQ IPLRLAIEAG SPQGWHRYVG SAGKVLAVEG
     FGASAPGDQV LREYGFTVEN VCRLALQLAG R
//
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