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Database: UniProt
Entry: K7W9E7_9NOST
LinkDB: K7W9E7_9NOST
Original site: K7W9E7_9NOST 
ID   K7W9E7_9NOST            Unreviewed;       670 AA.
AC   K7W9E7;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN   ORFNames=ANA_C13813 {ECO:0000313|EMBL:AFW96459.1};
OS   Anabaena sp. 90.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=46234 {ECO:0000313|EMBL:AFW96459.1, ECO:0000313|Proteomes:UP000010101};
RN   [1] {ECO:0000313|EMBL:AFW96459.1, ECO:0000313|Proteomes:UP000010101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90 {ECO:0000313|EMBL:AFW96459.1};
RX   PubMed=23148582; DOI=10.1186/1471-2164-13-613;
RA   Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C., Rantala-Ylinen A.,
RA   Vestola J., Jokela J., Rantasarkka K., Li Z., Liu B.;
RT   "Genome-derived insights into the biology of the hepatotoxic bloom-forming
RT   cyanobacterium Anabaena sp. strain 90.";
RL   BMC Genomics 13:613-613(2012).
CC   -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC       ketose donor to an aldose acceptor, via a covalent intermediate with
CC       the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC         ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001027,
CC         ECO:0000256|RuleBase:RU004996};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC       metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC       {ECO:0000256|RuleBase:RU004996};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU004996};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU004996}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131, ECO:0000256|RuleBase:RU004996}.
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DR   EMBL; CP003284; AFW96459.1; -; Genomic_DNA.
DR   RefSeq; WP_015081590.1; NC_019427.1.
DR   AlphaFoldDB; K7W9E7; -.
DR   STRING; 46234.ANA_C13813; -.
DR   KEGG; anb:ANA_C13813; -.
DR   PATRIC; fig|46234.3.peg.4340; -.
DR   eggNOG; COG0021; Bacteria.
DR   HOGENOM; CLU_009227_0_0_3; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000010101; Chromosome chANA01.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
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   NCBIfam; TIGR00232; tktlase_bact; 1.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU004996};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004996};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010101};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU004996};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT   DOMAIN          17..37
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
SQ   SEQUENCE   670 AA;  71443 MW;  07269FD330A63D66 CRC64;
     MAVATQSIQE LCINSIRFLA VDAIEKSKSG HPGLPMGAAP MAFVLWDSFM RYNPKNPQWF
     NRDRFVLSAG HGSMLQYALL YLTGYDSVTI DDIKQFRQWG AKTPGHPENF VTAGVEVTTG
     PLGQGIANAV GLAVAEAHLA AKFNKPDATI VDHYTYVILG DGCNMEGISG EAASIAGHWG
     LGKLIALYDD NHISIDGSTD VAFTEDVSKR FESYGWHVIH VKDGNTDLAG IAQAIEAAKA
     VTDKPTMIKV TTTIGYGSPN KQDTAGIHGA ALGPEETIAT RKNLGWEYDA FVVPEDALNH
     TRKAVERGAG YESAWNTVYA GYKAKYPQEA AEFDRFISGK LPEGWDQVLP TYTPEDKALP
     TRKHSENCLN KLGAVLPELI GGSADLTHSN LTELKGAGDF QKGHFANRNI HFGVREHAMG
     AICNGMALHN SGLIPYGATF LIFTDYMRAA IRLAALSEAG SIWVMTHDSI GQGEDGPTHQ
     PIETLASLRA IPDLTVIRPA DGNETSGGYK VAIEKSKAKA STLLAFTRQN VPNLAGTSIA
     GVAKGAYTIV DSEGTPDIIL IGTGSEVSLC VSAAEKLTAV GKKVRVVSMP SSTLFDTQDA
     AYKESVLPKA VTKRLSVEAA SSFGWHKYIG SEGDTVSIDT FGASAPGGIC LEKFGFTVDN
     VLAKAKALLG
//
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