ID A0A127A842_9MICC Unreviewed; 398 AA.
AC A0A127A842;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:AMM33842.1};
GN ORFNames=SA2016_3178 {ECO:0000313|EMBL:AMM33842.1};
OS Sinomonas atrocyanea.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Sinomonas.
OX NCBI_TaxID=37927 {ECO:0000313|EMBL:AMM33842.1, ECO:0000313|Proteomes:UP000070134};
RN [1] {ECO:0000313|EMBL:AMM33842.1, ECO:0000313|Proteomes:UP000070134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 3377 {ECO:0000313|EMBL:AMM33842.1,
RC ECO:0000313|Proteomes:UP000070134};
RA Kim K.M.;
RT "Complete genome of Sinomonas atrocyanea KCTC 3377.";
RL Submitted (FEB-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; CP014518; AMM33842.1; -; Genomic_DNA.
DR RefSeq; WP_066499862.1; NZ_CP014518.1.
DR AlphaFoldDB; A0A127A842; -.
DR STRING; 37927.SA2016_3178; -.
DR KEGG; satk:SA2016_3178; -.
DR PATRIC; fig|37927.3.peg.3263; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000070134; Chromosome.
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:AMM33842.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070134}.
FT DOMAIN 69..337
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 370..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 43387 MW; AAC2A445D2F78CE3 CRC64;
MTLPAEAQEA IRSFGISIED YMLPVHGRVP QIQILDEAGS LRPEDERGSA PGHEYPIPPA
EDLLEAYRRL VIGRRVNDQN SALVRQGRMA VYPSSHGQEA CQVAAALCLG AGDWMFPTYR
DAVAVMTRGV DPVETMTLFR GDWHGGYDPH AHKVGIQSTP LTTQLLHAVG VAHAAKLRGE
DTVVLAMCGD GATSEGDFHE ALNFAAVFNL PVVFFVQNNQ YAISVPLAHQ TVAPSIAHKA
VGYGMAGERV DGNDAVALLA VLDRAVRLAR AGSGPLLVEA YTYRMQAHTN ADDATRYRQD
AEVAAWAEKD PLKRMREYLR SEGVLAEETE AAFAADAEEV ARQLRDGLGA EAQPDPQDLF
RYVFTEPTPQ LREQAASLAE EQAREQSADE TTGEERRA
//
