(data stored in ACNUC6288 zone)

SWISSPROT: Q6BMN3_DEBHA

ID   Q6BMN3_DEBHA            Unreviewed;       678 AA.
AC   Q6BMN3;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 93.
DE   RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996};
GN   OrderedLocusNames=DEHA2F03960g {ECO:0000313|EMBL:CAG88854.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88854.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88854.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- 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
CC       divalent 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|RuleBase:RU004996}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|RuleBase:RU004996}.
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DR   EMBL; CR382138; CAG88854.1; -; Genomic_DNA.
DR   RefSeq; XP_460538.1; XM_460538.1.
DR   STRING; 4959.XP_460538.1; -.
DR   EnsemblFungi; CAG88854; CAG88854; DEHA2F03960g.
DR   GeneID; 2903189; -.
DR   KEGG; dha:DEHA2F03960g; -.
DR   HOGENOM; HOG000225953; -.
DR   InParanoid; Q6BMN3; -.
DR   KO; K00615; -.
DR   OMA; FADYMRG; -.
DR   OrthoDB; 354970at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
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; Q6BMN3.
DR   SWISS-2DPAGE; Q6BMN3.
KW   Calcium {ECO:0000256|RuleBase:RU004996};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Magnesium {ECO:0000256|RuleBase:RU004996};
KW   Metal-binding {ECO:0000256|RuleBase:RU004996};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU004996};
KW   Transferase {ECO:0000256|RuleBase:RU004996}.
FT   DOMAIN       14     34       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
SQ   SEQUENCE   678 AA;  73718 MW;  4B85A0BBCB8B678C CRC64;
     MSQDLDQLAI STIRLLSVDS VDKAQSGHPG APLGLAPAAH AVWQKMKFNP KDTNWINRDR
     FILSNGHACA LLYSLLVLYG YDLTVEDLKQ FRQLNSKTPG HPEALDVPGC EVTTGPLGQG
     ISNAVGLAMA QKQFGATYNK PDHKISDSYT YAFLGDGCLM EGVASETCSL AGHLQLNNLI
     AFWDDNHISI DGNTNVAFTE DVMLRFKAYG WHLIEIAEGD TDLDAIAKAI DEAKKVEDKP
     TLIRLTTTIG FGSLAQGTHG VHGAPLKADD IKQLKESMGF NPEETFVIPK EVTDYLKKHV
     EENQKVQEDW KKLFESYKQK YPELGAELQR RLDGKLPENW SDALPTYSPS DSAVATRKLS
     ETVLTKILPV IPEIIGGSAD LTGSNLTRAA GSVDFQPPAT GLGDYSGRYI RYGVREHGMG
     AIMNGIAAFG ANYKNYGGTF LNFVSYGAGA VRLSALSHHP VIWVATHDSI GLGEDGPTHQ
     PIETLAHLRA IPNLSVWRPA DGNETSAAYL QAIESTSTPS IIALTRQNLP QLEGSSIEKA
     AKGGYTLVKQ DKPDVIIVSS GSEVSISADA AKKLESEGFK AGVVSMPDFL TFDKQPLDYR
     LSVLPDGVPI MSVEVMSSFG WSKYSHEQFG LNRFGASGKG PEIYKFFEFT PEGVADRAAK
     TIQFYKGKPL LSPLNRAF
//

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