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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//