ID W6AAN0_9MOLU Unreviewed; 657 AA.
AC W6AAN0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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:AHI53910.1};
GN ORFNames=SSABA_v1c05030 {ECO:0000313|EMBL:AHI53910.1};
OS Spiroplasma sabaudiense Ar-1343.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276257 {ECO:0000313|EMBL:AHI53910.1, ECO:0000313|Proteomes:UP000019265};
RN [1] {ECO:0000313|EMBL:AHI53910.1, ECO:0000313|Proteomes:UP000019265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar-1343 {ECO:0000313|EMBL:AHI53910.1};
RX PubMed=24534435;
RA Chang T.H., Lo W.S., Ku C., Chen L.L., Kuo C.H.;
RT "Molecular evolution of the substrate utilization strategies and putative
RT virulence factors in mosquito-associated Spiroplasma species.";
RL Genome Biol. Evol. 6:500-509(2014).
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; CP006934; AHI53910.1; -; Genomic_DNA.
DR RefSeq; WP_025251050.1; NZ_CP006934.1.
DR AlphaFoldDB; W6AAN0; -.
DR STRING; 1276257.SSABA_v1c05030; -.
DR KEGG; ssab:SSABA_v1c05030; -.
DR PATRIC; fig|1276257.3.peg.513; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_14; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000019265; Chromosome.
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; 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:UP000019265};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 14..34
FT /note="Transketolase signature 1"
FT /evidence="ECO:0000259|PROSITE:PS00801"
SQ SEQUENCE 657 AA; 72438 MW; 252C9F9E24DC4B5E CRC64;
MVDNKKNKFL NSLRILGVEA VNKANSGHPG IILGAAPMVY ELYTKHINID PSNPKWFNRD
RFVLSAGHGS GLLYSILHLS GFGVEIDDLK KFRQLNSKTP GHPEFGMTDG VEVTTGPLGQ
GLAAAVGMAV AEKHLAGKFN KPELEVVNHF TYVLVGDGDL QEGIAQEAIS FAGNYGLNKL
IVLHDSNDIQ LDGPVKIAQS EKMQERFLAA NWNTILVKDG EDLAQISKAF ESAKKSTKPT
YIEVKTIIGL GATKQGTSAV HGEPVKDDLI NVKKYYNWTN PEFTIDEEVY AHYKATVGDR
GHEAYDQWNK IFNKYKQNYP QEFSQLEAGI LKQYQVTEAD FQAMIPSKPQ ATRVSSGQVL
DKISSLVPSF IGGSADLTAS TKAKGADGNF YQDNLQGRNI MYGVREFGMT AINNGIAAHS
GLLPFAGGFF VFSDYMKPAI RLAALMELQS FYVFTHDSVA VGEDGPTHEP VEQLAMLRSI
PGLNVFRPAD FQETYASYLT ALNDKNKPSA FILTRQDLPE LAHKDVVKNV GKGAYLISES
KNAQVTLIAT GSEVSLALKI KDELEKNQKL AVNVVSMVSM NIFDRQEKKY QDTIIQRNTQ
RFSIEMGTTF GWGKYLGDDG FAFGIDRFGH SAPGDQVIKE FGFTVENLTK KIIDKLK
//