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Database: UniProt
Entry: A0A1G1MZZ2_9BACT
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ID   A0A1G1MZZ2_9BACT        Unreviewed;       274 AA.
AC   A0A1G1MZZ2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:OGX22988.1};
GN   ORFNames=A3J51_03990 {ECO:0000313|EMBL:OGX22988.1};
OS   Omnitrophica WOR_2 bacterium RIFCSPHIGHO2_02_FULL_45_21.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1801854 {ECO:0000313|EMBL:OGX22988.1, ECO:0000313|Proteomes:UP000178464};
RN   [1] {ECO:0000313|EMBL:OGX22988.1, ECO:0000313|Proteomes:UP000178464}
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:OGX22988.1}.
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DR   EMBL; MHGN01000074; OGX22988.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1MZZ2; -.
DR   STRING; 1801854.A3J51_03990; -.
DR   Proteomes; UP000178464; Unassembled WGS sequence.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR049557; Transketolase_CS.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR47514; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR   PANTHER; PTHR47514:SF1; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          16..268
FT                   /note="Transketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00456"
SQ   SEQUENCE   274 AA;  30468 MW;  7040E8DDACD13239 CRC64;
     MSAIDEKDIK LLADKAKQLR RLIIKMLAQA GSGHPGGSLS AADIITCLYF KVMRYNPKEP
     NWPERDRFHM SKGHCCPALY AALSEAGYFP LEHLWTLRKF GSLLQGHPDR RTPGVEVASG
     SLGQGLSVAL GMALSGRIDK KNYRVYCLMG DGEIQEGNIW EAAMASAHYK CDQLCAVLDY
     NGFQIDGCIK EIMNLEPLVD KWRSFGWHTI EIDGHNIKEI LDALEEAKAI KGKPSIIIAH
     TIKGKGVSFM ENVLDFHGRA PTKEEAEKAL KELE
//
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