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Database: UniProt
Entry: A0A1F8MMY4_9CHLR
LinkDB: A0A1F8MMY4_9CHLR
Original site: A0A1F8MMY4_9CHLR 
ID   A0A1F8MMY4_9CHLR        Unreviewed;       314 AA.
AC   A0A1F8MMY4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:OGN99979.1};
GN   ORFNames=A2Y59_03070 {ECO:0000313|EMBL:OGN99979.1};
OS   Chloroflexi bacterium RBG_13_52_14.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797628 {ECO:0000313|EMBL:OGN99979.1, ECO:0000313|Proteomes:UP000180305};
RN   [1] {ECO:0000313|EMBL:OGN99979.1, ECO:0000313|Proteomes:UP000180305}
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   -!- 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:OGN99979.1}.
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DR   EMBL; MGMV01000146; OGN99979.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8MMY4; -.
DR   Proteomes; UP000180305; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
FT   DOMAIN          3..168
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   314 AA;  33827 MW;  4658FF9CDA76021A CRC64;
     MEQSTREAYG RTLVELGKQD PDIVVLDADL SKSTMTTFFA KEFPNRFFNC GIAEQNMIGI
     AAGLAASGKT AFASTFAVFA PGRCFDQIRM SVAQPGLNVK IVTSHSGITV GEDGTSHQAI
     EDLALICSLP SFTVIVPADA NEVVQAVKLA AQTYGPFYIR LSRPKTPLVY PSDYKFILGK
     ATTLREGKDI TIISTGIMVA YAMEAAQNLA KDGVDCRVLS MSTLKPLDTD AIVKAARETG
     AILTVEEHLR RGGLGSAVAQ IAAEHWPVPM SFMAIKDIYA KSGKAEELLK KHGLTAPDIE
     NAVRSLILRK RNNS
//
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