ID A0A1G0XV46_9BACT Unreviewed; 665 AA.
AC A0A1G0XV46;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=A2X48_04650 {ECO:0000313|EMBL:OGV37105.1};
OS Lentisphaerae bacterium GWF2_49_21.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798573 {ECO:0000313|EMBL:OGV37105.1, ECO:0000313|Proteomes:UP000178513};
RN [1] {ECO:0000313|EMBL:OGV37105.1, ECO:0000313|Proteomes:UP000178513}
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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:OGV37105.1}.
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DR EMBL; MHBH01000073; OGV37105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0XV46; -.
DR STRING; 1798573.A2X48_04650; -.
DR Proteomes; UP000178513; 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; 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; 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.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..35
FT /note="Transketolase signature 1"
FT /evidence="ECO:0000259|PROSITE:PS00801"
SQ SEQUENCE 665 AA; 72639 MW; 7666A04F823A1785 CRC64;
MSDYRLEKLS ADTIRVLSAE GVQKAKSGHP GMPMGCADFA FLLWYKYMKH NPKNPKWLGR
DRFVLSAGHG SPLLYTLLHL FEYNMPMEEL KNFRQWDSKT PGHPEFGHTE GVEVTTGPLG
SGFATGVGMA MAAKNFAART ELDKTSLMNN KIYILSSDGC MMEGTTHEAA SLAGHLKLDN
IICLYDDNSI TIEGSTSLAF TENVAMRYEA YGWRVIKIDN ANDLSKVDKG LAEALKSDGR
PTFVVCKTTI GFGSPNKAGK HSCHGEALGE EEVAATKAKL GMLSNPPFTV PAEVKDFVSK
RCQELASEAA KWDKEFQSFL EKNQDSAKLI SSLMNKTVPE NILQELIKAA PVDKPVATRV
SGGMVLNKVA DLVPALMGGA ADLTPSTKTN IKNTTSFTAT DRSGRNFHFG VRELGMGFLA
NGMVLYGTSI PYSATFFVFS DYMKPALRLA AIQNLHEIYV FTHDSFYVGE DGPTHEPIEQ
IVMLRTIPGM TVIRPAEANE VAHAWNVALK AKGPVALLLT RQDLEPIPPE LVKKIDVSKG
AYVLSEDAGF DLVMVATGSE VNLAFKAADL LRKEGRRVRV VSMPCIELFN AQDKSYRDSV
LPPSCRKRVT IEAGSTFGWK AFAGDDGLCI GLDHFGASAP YKVLADKFGF TPEKVVSSIK
AHFQS
//