ID X1EIZ9_9ZZZZ Unreviewed; 138 AA.
AC X1EIZ9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Transketolase C-terminal domain-containing protein {ECO:0000259|Pfam:PF02780};
DE Flags: Fragment;
GN ORFNames=S01H4_55067 {ECO:0000313|EMBL:GAH17094.1};
OS marine sediment metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=412755 {ECO:0000313|EMBL:GAH17094.1};
RN [1] {ECO:0000313|EMBL:GAH17094.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAH17094.1};
RX PubMed=24624126; DOI=10.3389/fmicb.2014.00080;
RA Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W.,
RA Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F.,
RA Takami H.;
RT "High frequency of phylogenetically diverse reductive dehalogenase-
RT homologous genes in deep subseafloor sedimentary metagenomes.";
RL Front. Microbiol. 5:80-80(2014).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
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:GAH17094.1}.
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DR EMBL; BART01031744; GAH17094.1; -; Genomic_DNA.
DR AlphaFoldDB; X1EIZ9; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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; IPR033248; Transketolase_C.
DR PANTHER; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 1.
DR Pfam; PF02780; Transketolase_C; 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 54..125
FT /note="Transketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02780"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GAH17094.1"
SQ SEQUENCE 138 AA; 15595 MW; 3B3211F8057F708D CRC64;
GWRIIAPSNA FDYIGLFNSS MISLDPVLII EHHALYDMTS PIPSGNLDYF VELGKAKPVA
EGSDVTLITY SNLVPRCENL LSQWAEENIS VELIDFRSLD YPSIDYHLIG ESVKKTGAVV
IVEEYRIVNM MPEPYLWI
//