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Database: UniProt
Entry: A0A1G0XV46_9BACT
LinkDB: A0A1G0XV46_9BACT
Original site: A0A1G0XV46_9BACT 
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
//
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