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Database: UniProt/TrEMBL
Entry: A9N311_SALPB
LinkDB: A9N311_SALPB
Original site: A9N311_SALPB 
ID   A9N311_SALPB            Unreviewed;       666 AA.
AC   A9N311;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   19-FEB-2014, entry version 43.
DE   RecName: Full=Transketolase;
DE            EC=2.2.1.1;
GN   OrderedLocusNames=SPAB_00478;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V.,
RA   Nash W., Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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; CP000886; ABX65911.1; -; Genomic_DNA.
DR   RefSeq; YP_001586744.1; NC_010102.1.
DR   ProteinModelPortal; A9N311; -.
DR   SMR; A9N311; 2-662.
DR   STRING; 272994.SPAB_00478; -.
DR   EnsemblBacteria; ABX65911; ABX65911; SPAB_00478.
DR   PATRIC; 18529003; VBISalEnt120821_0394.
DR   eggNOG; COG0021; -.
DR   HOGENOM; HOG000225953; -.
DR   OMA; WHVIGDI; -.
DR   OrthoDB; EOG6N3CRG; -.
DR   ProtClustDB; PRK12753; -.
DR   BioCyc; SENT28901:GH9O-476-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   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; 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   666 AA;  73069 MW;  1D76D66C89C04DEC CRC64;
     MSRKDLANAI RALSMDAVQK ANSGHPGAPM GMADIAEVLW NDFLKHNPTD PTWYDRDRFI
     LSNGHASMLL YSLLHLTGYD LPLEELKNFR QLHSKTPGHP EIGYTPGVET TTGPLGQGLA
     NAVGLAIAER TLGAQFNRPD HEIVDHYTYV FMGDGCLMEG ISHEVCSLAG TLGLGKLIGF
     YDHNGISIDG ETEGWFTDDT AKRFEAYHWH VVHDIDGHDP EAVKKAILEA QSVKDKPSLI
     ICRTVIGFGS PNKAGKEESH GAALGEEEVA LTRQKLGWHH PAFEIPKEIY RAWDGREKGE
     KAQQQWQEKF AAYEKAYPEL AAEFTRRMSG GLPEAWESAT QKFINDLQAN PAKIATRKAS
     QNTLNAYGPL LPELLGGSAD LAPSNLTIWK GSTSLKEDPA GNYIHYGVRE FGMTAIANGI
     AHHGGFVPYT ATFLMFVEYA RNAARMAALM KARQIMVYTH DSIGLGEDGP THQAVEQLAS
     LRLTPNFSTW RPCDQVEAAV GWKLAIERHH GPTALILSRQ NLAQVERTPE QVKAIARGGY
     ILKDSGGKPD IILIATGSEM EITLQAAEKL TGEGHNVRVV SLPSTDIFDA QDEAYRESVL
     PAHVTARVAV EAGIADYWYK YVGLKGAIIG MTGYGESAPA DKLFPYFGFT VENIVEKARR
     VLNIKG
//
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