ID   A0A1H7LJ57_9RHOB        Unreviewed;       334 AA.
AC   A0A1H7LJ57;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Pyruvate dehydrogenase E1 component alpha subunit {ECO:0000313|EMBL:SEK98954.1};
GN   ORFNames=SAMN04488526_1743 {ECO:0000313|EMBL:SEK98954.1};
OS   Jannaschia helgolandensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=188906 {ECO:0000313|EMBL:SEK98954.1, ECO:0000313|Proteomes:UP000199283};
RN   [1] {ECO:0000313|EMBL:SEK98954.1, ECO:0000313|Proteomes:UP000199283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14858 {ECO:0000313|EMBL:SEK98954.1,
RC   ECO:0000313|Proteomes:UP000199283};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; FNZQ01000002; SEK98954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7LJ57; -.
DR   STRING; 188906.SAMN04488526_1743; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000199283; 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:SEK98954.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199283}.
FT   DOMAIN          14..299
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   REGION          244..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  35894 MW;  86402DD7E8384431 CRC64;
     MTFANDAPLA RYRTMRRIRT FEERVGELFL KGESAGSMLH LSIGEEAVVG LTDHMAEGDT
     FTTHHRGHGI FLARGADPMR MLAEIAGREA GYCRGKGGSM HIADRGLGHL GANAIVGGGI
     PHVVGAGITA RNTGTRVVSV AFFGDGGMGQ GILYEAMNMA ALWKLPVVFC CINNQYGMGT
     RVDRSAGRQD FPARAEAFGL RAARADGSDV EAVHDAAQAI VEGARDGQPG FMEIDAYRFH
     GHARMDKSPY RTPEEEEEGR ARDPLATART SLADDTLLDT IDAEAEAEMD TAMKTAIAAT
     PPASDTMFQD VYDPSTPAPR PQRARLADVL EERA
//