ID W6A7C8_9MOLU Unreviewed; 654 AA.
AC W6A7C8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:AHI52886.1};
GN ORFNames=SCULI_v1c05450 {ECO:0000313|EMBL:AHI52886.1};
OS Spiroplasma culicicola AES-1.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276246 {ECO:0000313|EMBL:AHI52886.1, ECO:0000313|Proteomes:UP000019267};
RN [1] {ECO:0000313|EMBL:AHI52886.1, ECO:0000313|Proteomes:UP000019267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AES-1 {ECO:0000313|EMBL:AHI52886.1};
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; CP006681; AHI52886.1; -; Genomic_DNA.
DR RefSeq; WP_025363122.1; NZ_CP006681.1.
DR AlphaFoldDB; W6A7C8; -.
DR STRING; 1276246.SCULI_v1c05450; -.
DR KEGG; scq:SCULI_v1c05450; -.
DR PATRIC; fig|1276246.3.peg.543; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_14; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000019267; 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; 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; 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:UP000019267};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 348..518
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 654 AA; 72129 MW; 35EDE841CC1D140C CRC64;
MNKNNTNLNA LRILGIEAIN KANSGHPGIV LGAAPIVYTL FTKVMNINPN NPEWFNRDRF
VLSAGHGSGL LYSALHLSGF NLPLDEVKKF RQLNSLTPGH PEYKHTEGID STTGPLGQGF
AMAVGMALAE SHLAGKYNTK GQKIVDHYTY VLCGDGDLQE GVCQEAISFA GRYKLNKLIV
FHDSNDIQLD ARVEVAQSED MQARFKAANW NVLKIENGED LEAIEKAIAN AKKSDKPTYI
EVKTVIGLGA TNQGTQKVHG APLGNDIETV KKYFNWTQPE FEVSSEVYDF WKTNVATRGQ
AENEKWDQLF TQYAKENPQL ATQLQNAIVA KFEIDQTQLE ALNKKEEQAT RVSSGTVLNY
LSENIPSLIG GSADLTESTK AKGADGNYDF NALTGRNIMY GVREFAMGAI NNGIALHKGL
LPFASGFFVF SDYLKPAIRL SALMKIQALY IFTHDSIAVG EDGPTHQPIE QLAMLRSMPN
INVFRPCDMA ETQASYLAAI NDTTKPSVII ATRQNLKELE HNNVFEDVKK GAYLITKTDN
ANITLIASGS EVSLAMDVKN ILETKGHKVN VVSMVNMNEF NKQDRSYVDS IIDKNTTRFS
IELGSTFGWH KFLGDNGKAF GIDTFGYSAP FNDVINHIGF TADKISNEIL DIIK
//
