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Database: UniProt
Entry: A0A1F3H6Y2_9BACT
LinkDB: A0A1F3H6Y2_9BACT
Original site: A0A1F3H6Y2_9BACT 
ID   A0A1F3H6Y2_9BACT        Unreviewed;       331 AA.
AC   A0A1F3H6Y2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 10.
DE   SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:OFX86244.1};
GN   ORFNames=A2W86_03920 {ECO:0000313|EMBL:OFX86244.1};
OS   Bacteroidetes bacterium GWD2_45_23.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1797330 {ECO:0000313|EMBL:OFX86244.1, ECO:0000313|Proteomes:UP000178053};
RN   [1] {ECO:0000313|EMBL:OFX86244.1, ECO:0000313|Proteomes:UP000178053}
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:OFX86244.1}.
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DR   EMBL; MENT01000008; OFX86244.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F3H6Y2; -.
DR   Proteomes; UP000178053; Unassembled WGS sequence.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:OFX86244.1}.
FT   DOMAIN          24..321
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   331 AA;  36152 MW;  1219BC3ECB1AD0BA CRC64;
     MAKTSSKKVT DISKEKLLEM HRSMLDIRNF DNKVNRLVKR GVVPGMTHFS IGEEAANVGA
     VAALEIGSDL ITSNHRGHGQ SIALGINLNE MMAEIMGKAT GTCKGKGGSM HIADLDGGNL
     GANGIVGGGM GMAIGAALTQ KIKKTGKIVV CFFGDGAVNE GTFHETLNMA SIWKLPVIFY
     SINNMYGIST PISSVINIDY NYRRAASYGI PGHFIEDGND LMAVYNKFEE IVKYVREGNG
     PVLVESITYR YLGHSTSDPG KYRTKEEVDE WKKKDPILRF EQYLLDNKLV TKKDIEAIEK
     ASEDAVEESV KFALSSPEPT LESAFEDIFA P
//
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