TKT2_VIBPA
ID TKT2_VIBPA Reviewed; 663 AA.
AC Q87GY4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Transketolase 2;
DE Short=TK 2;
DE EC=2.2.1.1;
GN Name=tkt2; OrderedLocusNames=VPA1181;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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 ---------------------------------------------------------------------------
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; BA000032; BAC62524.1; -; Genomic_DNA.
DR RefSeq; NP_800691.1; NC_004605.1.
DR RefSeq; WP_005477253.1; NC_004605.1.
DR AlphaFoldDB; Q87GY4; -.
DR SMR; Q87GY4; -.
DR STRING; 223926.28809549; -.
DR EnsemblBacteria; BAC62524; BAC62524; BAC62524.
DR GeneID; 1191877; -.
DR KEGG; vpa:VPA1181; -.
DR PATRIC; fig|223926.6.peg.4107; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_6; -.
DR OMA; HHTEGIE; -.
DR Proteomes; UP000002493; Chromosome 2.
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; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..663
FT /note="Transketolase 2"
FT /id="PRO_0000191885"
FT ACT_SITE 410
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 113..115
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 436
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 25
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 259
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 663 AA; 72024 MW; 257C37A910491D93 CRC64;
MDRKYLANAI RALSMDGVQQ ANSGHPGAPM GMADIAEVLW RSHLNHNPSN PEWADRDRFV
LSNGHGSMLI YSLLHLSGYE LSIDDLKNFR QLHSKTPGHP EYGYAPGIET TTGPLGQGIT
NAVGMAMAEK ALAAQFNKEG HDIVDHFTYV FMGDGCLMEG ISHEACSLAG TLGLGKLIAF
WDDNGISIDG HVEGWFSDDT PKRFEAYGWH VIPAVDGHDA DAINAAIEAA KADPRPTLIC
TKTIIGFGSP NKSGSHDCHG APLGAEEIAA TRKELGWEHG PFEIPQEVYA EWSAKETGAA
KEAAWNEKFA AYEAAYPELA AEFKRRVNGE LPAEWEEKAS QIIADLQANP ANIASRKASQ
NALEAFGALL PEFMGGSADL APSNLTMWSG SKSLEANDFS GNYIHYGVRE FGMTAIMNGI
ALHGGFVPYG ATFLMFMEYA RNAMRMAALM KIQNIQVYTH DSIGLGEDGP THQPVEQIAS
LRLTPNMNTW RPCDQVESAV AWKLAIERKD APTALIFSRQ NLAQQPRSAE QVADIAKGGY
ILKDSEGKPE LILIATGSEV ELAVKAAEQL TAEGKKVRVV SMPSTDAFDK QDADYREAVL
PSDVTARIAI EAGIADFWYK YVGFDGRIIG MTTFGESAPA DQLFEMFGFT VENVVNTAKE
LLA
