GenomeNet

Database: UniProt
Entry: W6AAN0_9MOLU
LinkDB: W6AAN0_9MOLU
Original site: W6AAN0_9MOLU 
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}.
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; 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
//
DBGET integrated database retrieval system