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Database: UniProt
Entry: A0A418KTT4_9ACTN
LinkDB: A0A418KTT4_9ACTN
Original site: A0A418KTT4_9ACTN 
ID   A0A418KTT4_9ACTN        Unreviewed;       370 AA.
AC   A0A418KTT4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) E1 component subunit alpha {ECO:0000313|EMBL:RIQ29179.1};
GN   Name=pdhA {ECO:0000313|EMBL:RIQ29179.1};
GN   ORFNames=DY240_08500 {ECO:0000313|EMBL:RIQ29179.1};
OS   Jiangella rhizosphaerae.
OC   Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC   Jiangella.
OX   NCBI_TaxID=2293569 {ECO:0000313|EMBL:RIQ29179.1, ECO:0000313|Proteomes:UP000284057};
RN   [1] {ECO:0000313|EMBL:RIQ29179.1, ECO:0000313|Proteomes:UP000284057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-YY265 {ECO:0000313|EMBL:RIQ29179.1,
RC   ECO:0000313|Proteomes:UP000284057};
RA   Han C.;
RT   "Isolation, diversity and antifungal activity of actinobacteria from
RT   wheat.";
RL   Submitted (SEP-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:RIQ29179.1}.
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DR   EMBL; QUAL01000074; RIQ29179.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418KTT4; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000284057; 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:RIQ29179.1}.
FT   DOMAIN          54..323
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   370 AA;  39775 MW;  4E5121055768BF70 CRC64;
     MPTATSASAP PADAGLLPSA EPVRFLDDDG GPAPGDAHGR YERPSTELLR RAYDAMVLGR
     RFDAQATALT KQGRLAVYPS SRGQEAGEIG AVLALRETDW LFPTYRDTMA LIARGIDPVE
     ALTLLRGSWH CGYDPMATRT APQCTPLATH APHAVGVAHA ARRRGEDTVA LVLIGDGGTS
     EGDFHEALNF AAVFHAPVVF LVQNNGYAIS VPLSRQTAAP SLAHKGVGYG VRSERVDGND
     PLAMLAVLTD AVESARAGGG PVLVEAHTYR VEPHTNADDD ARYRDHDEVE AWKRRDPIAR
     LEAHLRSRGE LSDDDVAAAR SAAEEFATQV RERLSEEATG DPADLFAHVY AEPTPQLREQ
     AGWLAEELAR
//
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