ID A0A066UTC8_9VIBR Unreviewed; 663 AA.
AC A0A066UTC8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 Name=tkt {ECO:0000313|EMBL:KAB0300916.1};
GN ORFNames=F2Z80_17655 {ECO:0000313|EMBL:KAB0300916.1}, VFDL14_21130
GN {ECO:0000313|EMBL:KDN27394.1};
OS Vibrio fortis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=212667 {ECO:0000313|EMBL:KDN27394.1, ECO:0000313|Proteomes:UP000027219};
RN [1] {ECO:0000313|EMBL:KDN27394.1, ECO:0000313|Proteomes:UP000027219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dalian14 {ECO:0000313|EMBL:KDN27394.1,
RC ECO:0000313|Proteomes:UP000027219};
RA Wang Y., Song L., Liu G., Ding J.;
RT "Vibrio fortis Dalian14 Genome Sequencing.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAB0300916.1, ECO:0000313|Proteomes:UP000326687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7-72 {ECO:0000313|EMBL:KAB0300916.1,
RC ECO:0000313|Proteomes:UP000326687};
RA Das S.K.;
RT "Vibrio Fortis S7-72.";
RL Submitted (SEP-2019) 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:0000256|ARBA:ARBA00002931,
CC 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=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDN27394.1}.
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DR EMBL; VXDD01000003; KAB0300916.1; -; Genomic_DNA.
DR EMBL; JFFR01000027; KDN27394.1; -; Genomic_DNA.
DR RefSeq; WP_032552751.1; NZ_VXDD01000003.1.
DR AlphaFoldDB; A0A066UTC8; -.
DR STRING; 212667.VFDL14_21130; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000027219; Unassembled WGS sequence.
DR Proteomes; UP000326687; Unassembled WGS sequence.
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; IPR049557; Transketolase_CS.
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|ARBA:ARBA00022837, 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 353..524
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 663 AA; 71700 MW; 7D357C7B4FFDD713 CRC64;
MDRKHLANAI RALSMDGVQQ ANSGHPGAPM GMADIAEVLW RDHLNHNPSN PEWADRDRFV
LSNGHGSMLI YSLLHLAGYE LSIEDLKNFR QLHSKTPGHP EYGYAPGIET TTGPLGQGIT
NAVGMALAEK TLAAQFNKEG HDIVDHFTYA FMGDGCLMEG ISHEACSLAG TLGLGKLIAF
WDDNGISIDG EVEGWFSDDT PKRFEAYGWH VIPAVDGHNA EAINAAIEAA KADPRPTLIC
TKTIIGFGSP NKSGSHDCHG APLGAEEIAA TRKELGWEHG PFEIPSEVYA EWDAKEAGAA
KEAAWNEKLA AYEAAHPELA AEFKRRVNGE LPAQWEEKAN QIIADLQANP ANIASRKASQ
NALEAFGAML PEFLGGSADL APSNLTMWSG SKSVSAEDPA GNYIHYGVRE FGMTAIMNGI
ALHGGFVPYG ATFLMFMEYA RNAMRMAALM KVQNIQVYTH DSIGLGEDGP THQPVEQMAS
LRLTPNMSTW RPCDQVESAV AWKLAIERKD GPTSLIFSRQ NLAQQERSEE QVANIAKGGY
ILKDCEGKPE LILIATGSEV ELAVNAAAEL TAEGKKVRVV SMPATDAFDK QDAEYRESVL
PSDVTARIAV EAGIADFWYK YVGFGGKIIG MTTFGESAPA GELFKMFGFT TENVVNTAKE
LLA
//
