ID A0A1G6ZY46_9PROT Unreviewed; 667 AA.
AC A0A1G6ZY46;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ORFNames=SAMN04488071_2011 {ECO:0000313|EMBL:SDE07588.1};
OS Kordiimonas lacus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales;
OC Kordiimonadaceae; Kordiimonas.
OX NCBI_TaxID=637679 {ECO:0000313|EMBL:SDE07588.1, ECO:0000313|Proteomes:UP000183685};
RN [1] {ECO:0000313|EMBL:SDE07588.1, ECO:0000313|Proteomes:UP000183685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9109 {ECO:0000313|EMBL:SDE07588.1,
RC ECO:0000313|Proteomes:UP000183685};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|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=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=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}.
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DR EMBL; FNAK01000004; SDE07588.1; -; Genomic_DNA.
DR RefSeq; WP_068304149.1; NZ_LRUA01000003.1.
DR AlphaFoldDB; A0A1G6ZY46; -.
DR STRING; 637679.GCA_001550055_01846; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000183685; 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|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 Reference proteome {ECO:0000313|Proteomes:UP000183685};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 358..530
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 667 AA; 71865 MW; 3077DC5823E8D2AA CRC64;
MPDTDIQQDD ILNQKMANAI RALSMDAVQK ANSGHPGMPM GMADVATVLF SKFMRFDPKW
PTWPNRDRFV LSAGHGSMLI YSLLHLTGYE RPTMEDIKNF RQLHSPTAGH PEFGECPGVE
TTTGPLGQGL ATSVGMAIAE RLSNEEYGDD ITDHFTYVLA GDGCLMEGVS QEAISLAGHL
KLSKMIVLWD DNSISIDGST DLSTSEDQAM RFEAAGWHVQ AVDGHDMESI EAAIAEAQRA
DQPSLIACRT TIGYGAPNKQ GTAATHGAPL GDDEIKAARE FLGWDHAPFE IPEDVLAAWR
AVGEAGASLS ADWKAKFETL DGFVKEDFER RLNKDLPKGF AAAINDYKAK LAAEPVKVAT
RKASQMALEV VNGVVPETIG GSADLTGSNL TKTSQTDGIT ADDFSGRYMY YGIREFEMCA
AMNGIALYNQ HIPYGGTFMV FTDYARPAIR LAALMKQRSI YVMTHDSIGL GEDGPTHQPV
EHLPALRAMP NLNVFRPCDA VETAECWALA LEAKETPSVL SLTRQSTIQQ RLEHTDENLC
AKGGYVLHEA STGAPKVVLI ASGSEVELAA AARETLEADG VPTRVVSMPS TELFDAQDAA
YKASVLPEGT VRGSIEAAST YGWAKYTGLD GVNIGIDSFG ASAPAEDLYK HFGITSDALV
AAVREKL
//
