ID   A0A1G3Z166_9BACT        Unreviewed;       666 AA.
AC   A0A1G3Z166;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   25-APR-2018, entry version 6.
DE   RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996};
GN   ORFNames=A2007_05165 {ECO:0000313|EMBL:OHE70577.1};
OS   Verrucomicrobia bacterium GWC2_42_7.
OC   Bacteria; Verrucomicrobia; unclassified Verrucomicrobia.
OX   NCBI_TaxID=1802430 {ECO:0000313|EMBL:OHE70577.1};
RN   [1] {ECO:0000313|EMBL:OHE70577.1}
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.,
RA   Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected
RT   biogeochemical processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from
CC       a ketose donor to an aldose acceptor, via a covalent intermediate
CC       with the cofactor thiamine pyrophosphate.
CC       {ECO:0000256|RuleBase:RU004996}.
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
CC       {ECO:0000256|RuleBase:RU004996}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU004996}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|RuleBase:RU004996, ECO:0000256|SAAS:SAAS00651207}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OHE70577.1}.
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DR   EMBL; MIDO01000131; OHE70577.1; -; Genomic_DNA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
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|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651250};
KW   Metal-binding {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651225};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651235};
KW   Transferase {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651241}.
FT   DOMAIN       22     42       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                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
//