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Database: UniProt
Entry: A0A495W6A5_9PSEU
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ID   A0A495W6A5_9PSEU        Unreviewed;       355 AA.
AC   A0A495W6A5;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   13-SEP-2023, entry version 13.
DE   SubName: Full=Pyruvate dehydrogenase E1 component alpha subunit {ECO:0000313|EMBL:RKT56193.1};
GN   ORFNames=C8E97_4882 {ECO:0000313|EMBL:RKT56193.1};
OS   Saccharothrix australiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=2072 {ECO:0000313|EMBL:RKT56193.1, ECO:0000313|Proteomes:UP000282084};
RN   [1] {ECO:0000313|EMBL:RKT56193.1, ECO:0000313|Proteomes:UP000282084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43800 {ECO:0000313|EMBL:RKT56193.1,
RC   ECO:0000313|Proteomes:UP000282084};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RKT56193.1}.
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DR   EMBL; RBXO01000001; RKT56193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495W6A5; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000282084; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; IPR017596; PdhA/BkdA.
DR   InterPro; IPR029061; THDP-binding.
DR   NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR   PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 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:RKT56193.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282084}.
FT   DOMAIN          44..310
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   355 AA;  38219 MW;  DFEE80F1CF323EAD CRC64;
     MSPTRERTLL PTDEPLSLLD KDGSPVAGSP LVMPDDDVLL ELHRRMVVGR RFDTQATALT
     RQGRLAVYPS SRGQEACEVG SVLALRPADW LFPTYRDTVA LVTRGVDPAE ALTLLQGDWH
     SGYDPCAHRV GPQCTPLATN TLHAVGFAHA ARLKGEDTSV LVLLGDGATS EGDTHEALNF
     AGVWRAPVVF LVQNNGYAIS VPMSKQNAAP SLAHKGIGYG VPSVLVDGND VAAVYAVVRE
     ALESGGPTLI EARTYRIEAH TNADDATRYR TPDEVAAWLD RDPVDRIEAY LTSRGLLDAA
     RRSAVAAEAE EFAARVRAEL NADRPRDPAA LFEHVYATPT AQLREQAAAL AEELA
//
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