ID A0A1B1ANW1_9ACTN Unreviewed; 400 AA.
AC A0A1B1ANW1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) E1 component subunit alpha {ECO:0000313|EMBL:ANP48241.1};
GN ORFNames=AVL59_00455 {ECO:0000313|EMBL:ANP48241.1};
OS Streptomyces griseochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68214 {ECO:0000313|EMBL:ANP48241.1, ECO:0000313|Proteomes:UP000092659};
RN [1] {ECO:0000313|EMBL:ANP48241.1, ECO:0000313|Proteomes:UP000092659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14511 {ECO:0000313|EMBL:ANP48241.1,
RC ECO:0000313|Proteomes:UP000092659};
RA Wu L.;
RT "Complete genome sequence of Streptomyces griseochromogenes ATCC 14511, the
RT Blasticidin S producer.";
RL Submitted (JUN-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; CP016279; ANP48241.1; -; Genomic_DNA.
DR RefSeq; WP_067299227.1; NZ_JAGGLP010000007.1.
DR AlphaFoldDB; A0A1B1ANW1; -.
DR STRING; 68214.AVL59_00455; -.
DR KEGG; sgs:AVL59_00455; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000092659; 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:ANP48241.1}.
FT DOMAIN 76..356
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 43942 MW; 1CB3B6BC6E97E160 CRC64;
MTVDSSAARK PRRSAAGKAG TTGSRTGTTG TKRTTKKSTD PELVQLLTPE GKRVKNAEYD
GYVAQITADE LRGLYRDMVL TRRFDAEATA LQRQGELGLW ASLLGQEAAQ IGSGRALRDD
DYVFPTYREH GVAWCRGVDP TNLLGMFRGV NNGGWDPNSN NFHLYTIVIG SQTLHATGYA
MGITKDGADS AVIAYFGDGA SSQGDVAESF TFSAVYNAPV VFFCQNNQWA ISEPTEKQSR
VPLYQRAQGF GFPGVRVDGN DVLACLAVTK WALERARNGE GPTLVEAYTY RMGAHTTSDD
PTRYRGDEER LAWEAKDPIL RLRRYLEVSN HADEGFFAEL ESESEALGRR VREAVRAMPD
PDHFAIFENV YADGHALVDE ERAQFAAYQA SFADAEAEGV
//
