ID   A0A1G3Z166_9BACT        Unreviewed;       666 AA.
AC   A0A1G3Z166;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   29-SEP-2021, entry version 16.
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=A2007_05165 {ECO:0000313|EMBL:OHE70577.1};
OS   Verrucomicrobia bacterium GWC2_42_7.
OC   Bacteria; Verrucomicrobia.
OX   NCBI_TaxID=1802430 {ECO:0000313|EMBL:OHE70577.1, ECO:0000313|Proteomes:UP000184561};
RN   [1] {ECO:0000313|EMBL:OHE70577.1, ECO:0000313|Proteomes:UP000184561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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   -!- 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:OHE70577.1}.
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DR   EMBL; MIDO01000131; OHE70577.1; -; Genomic_DNA.
DR   Proteomes; UP000184561; 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; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
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   PANTHER; PTHR43522; PTHR43522; 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; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00232; tktlase_bact; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU004996};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT   DOMAIN          22..42
FT                   /note="TRANSKETOLASE_1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
SQ   SEQUENCE   666 AA;  72674 MW;  24D71C155AF6EBCF CRC64;
     MKKNNIIATK EEMLKKAAQE ARGLAIDAVS SAKSGHLGLP LGAAEIGAVL FGQLLHYNPD
     EPRWLNRDRF VLSAGHGSMF LYAWLHLAGY DLSLDEIRHF RQLNSKTPGH PEFRMTPGVE
     CTTGPLGQGI GNAVGMAISA KMMAARYNTS CQLFDYSVVC LCGDGCLQEG VAQEAIAFAG
     HLGLDNLILI YDSNGVTLDA MADKTQSGNV VKRFESYGFD VQQVDGHDMV AIAKAYESAK
     NAKNQKPHLI IATTVIGKGI AEVEGTAKAH GEGGFKFADA ARRSLGLPSE KFFVSQEVRN
     FFEGHRFNLL STYTKWKDMF AQWSKANPSL AQELSSTLPP PPPYDLLNKI PCFTEETLST
     RVAGEKVLNA LASFDPLIIS VSADLHSSTK NYIHNGGDIF KNSFSGKNLC FGIREHAMGA
     ILNGFAYEGI FKPSGATFLV FSDYLRPSIR LAALSHLPVV YIFTHDSIGV GEDGPTHQPI
     ETISALRCIP NLHVIRPADC EETVGAFIAA MDRMSGPTAL ILTRQNIPNL HTINADTRRH
     SVAKGAYVAK KEKGELKLIL MASGSEVHLA LKVAEELDDN VRVVSMPSME LFDRQSDSYK
     QQILPSSCKN RISIEAGRTS LWHKYVGLEG VVMGIDKFGI SAPAELIFQS YGLTMDNILK
     EAKNFL
//