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TKT_AQUAE
ID   TKT_AQUAE               Reviewed;         689 AA.
AC   O67642;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Transketolase;
DE            Short=TK;
DE            EC=2.2.1.1;
GN   Name=tkt; Synonyms=tktA; OrderedLocusNames=aq_1765;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
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+). {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR   EMBL; AE000657; AAC07607.1; -; Genomic_DNA.
DR   PIR; H70451; H70451.
DR   RefSeq; NP_214208.1; NC_000918.1.
DR   AlphaFoldDB; O67642; -.
DR   SMR; O67642; -.
DR   STRING; 224324.aq_1765; -.
DR   EnsemblBacteria; AAC07607; AAC07607; aq_1765.
DR   KEGG; aae:aq_1765; -.
DR   PATRIC; fig|224324.8.peg.1361; -.
DR   eggNOG; COG0021; Bacteria.
DR   HOGENOM; CLU_009227_0_0_0; -.
DR   InParanoid; O67642; -.
DR   OMA; HHTEGIE; -.
DR   OrthoDB; 188169at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IBA:GO_Central.
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; 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.
PE   3: Inferred from homology;
KW   Calcium; Magnesium; Metal-binding; Reference proteome;
KW   Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..689
FT                   /note="Transketolase"
FT                   /id="PRO_0000191850"
FT   ACT_SITE        434
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         144..146
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         380
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         460
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         484
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         492
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         543
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            56
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            289
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   689 AA;  77982 MW;  285A8EAADEA20D47 CRC64;
     MVVQLDQIHF FIFHEVLKIF KTMPQLFKTS KKIDELVINT IRFLSVDMVE RAKSGHPGMP
     LGASHIVYLL YDRIMKYNPK NPNWFNRDRF ILSAGHGSAM LYAAFYMFGF DLTLEDLKAF
     RQLNSKTPGH PEYGLTPGVE VTTGNLGQGF GNAVGMAMAE KFLSHYFNRE GYPVIDHYTY
     VLVSDGDLME GVSYEAASLA GHFKLNKLIA IWDNNHITID GDTKLTWTED VLKRFEALGW
     EVYHLEDGYN LDLLEETILK AKESDKPTFI SVRTHIGYGT PLQDTPEVHG KPMGKEIVEE
     TKKKFGWPLE EFYVPEEALN YTRRKVEEGK ALEEEWNKLY AEYREKYPDL AQTLEKALNK
     EWSLDWLEKV EEFKEDMPTR KASGKVLNVM ADYIPTMIGG SADLSESVNT VLKKYGDFEA
     DTPTGRNVHY GVREHAMGTI LNGMAYHGGI LPYGGTFLIF SEYMRPAIRT AALANLQVIF
     VYSHDSIGLG EDGPTHQPVE QLWSLRSIPN LWVVRPADAN EVKYAWEIAL KRKNGPTAII
     LTRQKVKTID RSKYASPEGV RKGAYVIADT EGKPDVVIIA TGSEVQVALG AKEILEQKGI
     KTRVVNMACC ELFEEQPEEY KREVLPPEVT KRVAVEAGRD TGWYKYVGSD GLVISLNEFG
     KSAPGSVLFE YYGFTPENVA NKVIEKWFS
 
 
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