ID A0A0Q7N2S3_9NOCA Unreviewed; 360 AA.
AC A0A0Q7N2S3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) E1 component subunit alpha {ECO:0000313|EMBL:KQY33670.1};
GN ORFNames=ASD42_14125 {ECO:0000313|EMBL:KQY33670.1};
OS Nocardia sp. Root136.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1736458 {ECO:0000313|EMBL:KQY33670.1, ECO:0000313|Proteomes:UP000051507};
RN [1] {ECO:0000313|Proteomes:UP000051507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root136 {ECO:0000313|Proteomes:UP000051507};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY33670.1, ECO:0000313|Proteomes:UP000051507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root136 {ECO:0000313|EMBL:KQY33670.1,
RC ECO:0000313|Proteomes:UP000051507};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQY33670.1}.
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DR EMBL; LMFE01000007; KQY33670.1; -; Genomic_DNA.
DR RefSeq; WP_056819156.1; NZ_LMFE01000007.1.
DR AlphaFoldDB; A0A0Q7N2S3; -.
DR STRING; 1736458.ASD42_14125; -.
DR Proteomes; UP000051507; 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:KQY33670.1}.
FT DOMAIN 41..310
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 360 AA; 39546 MW; 34B3B34667AFF476 CRC64;
MSQKQTYPVQ LVQPDGRRVF DKAHAALVAD IDAARLRQLY RDMVVTRRID VEATALQRQG
QLGLWPPLLG QEAAQVGSAH ALHPDDYVFC SYRESAVAYC RGVPPEQLTA LWRGASHHCW
DPTEFNITNA NIVVGSQGLH ATGYAYAAHL DGADIATIAY FGDGATSTGD IAEALGFAAA
WSAPVVFFCQ NNHWAISEPV TVQSNVALVR RADGYGIPGV QVDGNDVLAV LAVTRQAVER
ARTGGGPTFI EAMTYRMGPH TTADDPTRYR TAADTEYWAQ RDPIDRVRLL LEREGHLSPE
LAQQVTDEAD DVARRLRAAT IEMPDPDPER MFDNVYATEH PLMTEERQQL SAYLAEGAQS
//
