ID A0A1F9KIZ8_9DELT Unreviewed; 335 AA.
AC A0A1F9KIZ8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=A3F90_18665 {ECO:0000313|EMBL:OGQ79681.1};
OS Deltaproteobacteria bacterium RIFCSPLOWO2_12_FULL_60_19.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1797894 {ECO:0000313|EMBL:OGQ79681.1, ECO:0000313|Proteomes:UP000177611};
RN [1] {ECO:0000313|EMBL:OGQ79681.1, ECO:0000313|Proteomes:UP000177611}
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 -!- 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 -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
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:OGQ79681.1}.
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DR EMBL; MGSS01000116; OGQ79681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F9KIZ8; -.
DR STRING; 1797894.A3F90_18665; -.
DR Proteomes; UP000177611; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_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; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 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;
KW Pyruvate {ECO:0000313|EMBL:OGQ79681.1}.
FT DOMAIN 13..188
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 335 AA; 35780 MW; 70D8CCDA288618DE CRC64;
MKAPAQQATV REITFGQAIN EALAEEMRRD LRVFIIGEDV AEAGTPFKVL SGLVRQFGPE
RVIDSPISEA GIAGIGVGAA MTGMRPVVDI MFGDFVTLIM DQVVNQAAKI HYMSGGKLKV
PLVIRTTLGA TRRSAAQHSQ SLHAWFSHIP GLKVAVPSTP YDAKGLLKSA IRDDNPVIIF
EDKLMYQLKG PVPDDDYTIP FGVADIKRAG TDITMVATSS MVQVALAAAG MLEKEGISAE
VVDVRTTAPL DKETIVESAK KTSRAIVIDE GYERYGVTAE IAAVIAEGAF YNLDAPVKRM
GAMDVPVPFS PALEDLTVPT PESVAEAAKK LCGKP
//
