位置:首页 > 蛋白库 > TKT1_VIBVU
TKT1_VIBVU
ID   TKT1_VIBVU              Reviewed;         664 AA.
AC   Q8DCA2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Transketolase 1;
DE            Short=TK 1;
DE            EC=2.2.1.1;
GN   Name=tkt1; OrderedLocusNames=VV1_1537;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO09963.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016795; AAO09963.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043920938.1; NC_004459.3.
DR   AlphaFoldDB; Q8DCA2; -.
DR   SMR; Q8DCA2; -.
DR   EnsemblBacteria; AAO09963; AAO09963; VV1_1537.
DR   KEGG; vvu:VV1_1537; -.
DR   HOGENOM; CLU_009227_0_1_6; -.
DR   OMA; NSGHSGM; -.
DR   Proteomes; UP000002275; Chromosome 1.
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;
KW   Calcium; Magnesium; Metal-binding; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..664
FT                   /note="Transketolase 1"
FT                   /id="PRO_0000191886"
FT   ACT_SITE        411
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         114..116
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
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         185
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         384
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         437
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         461
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         469
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         520
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            26
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            260
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   664 AA;  71833 MW;  5F285D626C49AD8C CRC64;
     MPSRKHLANA IRALSMDGVQ KANSGHPGAP MGMADIAEVL WRGHLNHNPS NPEWADRDRF
     VLSNGHGSML IYSLLHLSGY ELSIDDLKNF RQLHSKTPGH PEYGYAPGIE TTTGPLGQGI
     TNAVGMAMAE KALAAQFNKP GHDIVDHFTY VFMGDGCLME GISHEACSLA GTLGLGKLIA
     FWDDNGISID GHVEGWFSDD TPKRFEAYGW HVIPAVDGHN AEAINAAIEA AKADPRPTLI
     CTKTIIGFGS PNKSGSHDCH GAPLGAEEIA AAREFLGWEH PAFEIPADVY AEWDAKAAGA
     EKEAAWNAKF DAYAAAYPTE AAELKRRLNG ELPAEWEEKA NQIIADLQAN PANIASRKAS
     QNALEAFGKM LPEFMGGSAD LAPSNLTMWS GSKSLEANDF SGNYIHYGVR EFGMTAIMNG
     IALHGGFVPY GATFLMFMEY ARNAMRMAAL MKVQNIQVYT HDSIGLGEDG PTHQPVEQIA
     SLRLTPNMST WRPCDQVESA VAWKLAIERK DGPSALIFSR QNLAQQPRSA EQVADIAKGG
     YILKDSDGKP ELILIATGSE VELAVKAAEQ LTAEGKKVRV VSMPATDTFD KQDAAYREAV
     LPSDVTARIA IEAGIADFWY KYVGFDGRII GMTTFGESAP ADQLFEMFGF TVENVVNTAK
     ELLA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024