(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NUW7_YERPA

ID   A0A0E1NUW7_YERPA        Unreviewed;       664 AA.
AC   A0A0E1NUW7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 24.
DE   RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996};
GN   OrderedLocusNames=YPA_0340 {ECO:0000313|EMBL:ABG12308.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12308.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12308.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12308.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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.
CC       {ECO:0000256|RuleBase:RU004996}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-
CC         phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-
CC         phosphate; Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483,
CC         ChEBI:CHEBI:57737, ChEBI:CHEBI:58273, ChEBI:CHEBI:59776;
CC         EC=2.2.1.1; Evidence={ECO:0000256|RuleBase:RU004996};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU004996}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|RuleBase:RU004996, ECO:0000256|SAAS:SAAS01133303}.
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DR   EMBL; CP000308; ABG12308.1; -; Genomic_DNA.
DR   RefSeq; WP_002209965.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12308; ABG12308; YPA_0340.
DR   EnsemblBacteria; AJJ80759; AJJ80759; CH58_3188.
DR   KEGG; ypa:YPA_0340; -.
DR   PATRIC; fig|360102.15.peg.3346; -.
DR   KO; K00615; -.
DR   OMA; FADYMRG; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR005478; Transketolase_bac-like.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43522; PTHR43522; 1.
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;
DR   PRODOM; A0A0E1NUW7.
DR   SWISS-2DPAGE; A0A0E1NUW7.
KW   Calcium {ECO:0000256|RuleBase:RU004996};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Magnesium {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS01130536};
KW   Metal-binding {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS01130540};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS01133301};
KW   Transferase {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00460013, ECO:0000313|EMBL:ABG12308.1}.
SQ   SEQUENCE   664 AA;  71873 MW;  D01E58B790CB1F09 CRC64;
     MSSRKELANA IRALSMDAVQ KAKSGHPGAP MGMADIAEVL WRDYLNHNPT NPHWADRDRF
     VLSNGHGSML IYSLLHLTGY DLPMEELKNF RQLHSKTPGH PEYGYTAGVE TTTGPLGQGI
     ANAVGFAIAE RTLGAQFNRP GHDIVDHHTY AFMGDGCMME GISHEVCSLA GTMKLGKLTA
     FYDDNGISID GHVEGWFTDD TAARFEAYGW HVVRGVDGHN ADSIKAAIEE AHKVTDKPSL
     LMCKTIIGFG SPNKAGTHDS HGAPLGEAEV AATREALGWK YPAFEIPQDI YAAWDAKEAG
     KAKEAAWNEK FAAYAKAYPE LAAEFKRRVS GELPANWAVE SKKFIEQLQA NPANIASRKA
     SQNALEAFGK VLPEFLGGSA DLAPSNLTIW SGSKSLSDDL AGNYIHYGVR EFGMSAIMNG
     IALHGGFIPY GATFLMFVEY ARNAVRMAAL MKIRSVFVYT HDSIGLGEDG PTHQPVEQMA
     SLRVTPNMST WRPCDQVESA VAWQYALERK DGPSALIFSR QNLAQQPRTA EQLANIAKGG
     YVLKDCAGQP ELILIATGSE VELAVAAADQ LTATGRKVRV VSMPSTDAFD KQDAAYRESV
     LPSAVSARVA VEAGIADYWY KYVGLNGAVV GMTTFGESAP AELLFKEFGF TVENVVAKAQ
     ALLK
//

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