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Database: UniProt
Entry: E8NGA7_MICTS
LinkDB: E8NGA7_MICTS
Original site: E8NGA7_MICTS 
ID   E8NGA7_MICTS            Unreviewed;       371 AA.
AC   E8NGA7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, eukaryotic type, alpha subunit {ECO:0000313|EMBL:BAJ76578.1};
GN   OrderedLocusNames=MTES_3614 {ECO:0000313|EMBL:BAJ76578.1};
OS   Microbacterium testaceum (strain StLB037).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ76578.1, ECO:0000313|Proteomes:UP000008975};
RN   [1] {ECO:0000313|EMBL:BAJ76578.1, ECO:0000313|Proteomes:UP000008975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB037 {ECO:0000313|EMBL:BAJ76578.1,
RC   ECO:0000313|Proteomes:UP000008975};
RX   PubMed=21357489; DOI=10.1128/JB.00180-11;
RA   Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT   lactone-degrading bacterium isolated from potato leaves.";
RL   J. Bacteriol. 193:2072-2073(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=StLB037;
RA   Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037.";
RL   Submitted (FEB-2011) 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; AP012052; BAJ76578.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8NGA7; -.
DR   STRING; 979556.MTES_3614; -.
DR   KEGG; mts:MTES_3614; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_1_0_11; -.
DR   Proteomes; UP000008975; 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:BAJ76578.1}.
FT   DOMAIN          53..323
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   371 AA;  40148 MW;  3A0A1E3ACE840F9B CRC64;
     MTYTQTQDSV TGGVPDEGDV LRVLEPDGAR VPDATLEPWI ADLSPHELRA LHRDMVLTRR
     LDAEGVALQR QGQLALWAPC RGQEAVQVGT AHALAPGDFV FPSYREHGVL LGRGAQPADY
     VLAWRGEEHS AYDHRAINAA PPQIIIGAQS LHATGWAMGA QRDGSTDVAV AYYGDGATSQ
     GDVNEAMVFA SSFGAPVVFV CSNNQWAISE PVTVQAKYPI AGRAPGFGIP SLRIDGNDAL
     ACVAAMRWAL DRARRGEGPS FIEAVTYRMG PHTTSDDPTR YRDAAEVEEW TQRDPIARLE
     AYLRAEGMLD DSGMAEVARA ADALAAEVRT ACIGATTRAP ETMFDHVYAE PHAGLERQRA
     EYVAYLEGFE K
//
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