ID A0A1Q5CDA0_9ACTN Unreviewed; 390 AA.
AC A0A1Q5CDA0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) E1 component subunit alpha {ECO:0000313|EMBL:OKI81564.1};
GN ORFNames=A6A27_15775 {ECO:0000313|EMBL:OKI81564.1};
OS Micromonospora sp. CB01531.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI81564.1, ECO:0000313|Proteomes:UP000186700};
RN [1] {ECO:0000313|EMBL:OKI81564.1, ECO:0000313|Proteomes:UP000186700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01531 {ECO:0000313|EMBL:OKI81564.1,
RC ECO:0000313|Proteomes:UP000186700};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(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:OKI81564.1}.
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DR EMBL; LWLS01000024; OKI81564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5CDA0; -.
DR STRING; 1718947.A6A27_15775; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000186700; 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:OKI81564.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186700}.
FT DOMAIN 66..339
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 42560 MW; 481B22A22CF20363 CRC64;
MTTTPQAVRR ASPRTRRKAT PAAVDPSAGL LPRTEPVRLL NPDGTPLPAR DDYPEPPLDA
LREMYRRMVV GRRFDVQATA LTKQGRLAVY PSSRGQEACQ VGGVLALHDT DWVFPTYRES
MALTARGIDP VEVLTLLRGD WHCGYDPAAR HTAPQCTPLA TQCVHAAGLA YGESYQGRDT
VALAFIGDGA TSEGDFHEGV NFAAVFKAPV VYFVQNNKYA ISVPLSRQTA APSLAYKGVG
YGVPSEQVDG NDPVAVLAVL TRAVEHARSG QGPFLVEAHT YRMEPHTNAD DQTRYRDAEE
VEAWRDRDPI ARLETYLRAR GVLDDAAVAA IADEAEAYAA ALRDRMNAQP AVDPLSLFDH
VYAEPTPQLV EQREQVRAEL AAARDEEGDA
//
