ID A0A066Z255_9ACTN Unreviewed; 383 AA.
AC A0A066Z255;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Pyruvate dehydrogenase E1 subunit alpha {ECO:0000313|EMBL:KDN84225.1};
GN ORFNames=KCH_40160 {ECO:0000313|EMBL:KDN84225.1};
OS Kitasatospora cheerisanensis KCTC 2395.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN84225.1, ECO:0000313|Proteomes:UP000027178};
RN [1] {ECO:0000313|EMBL:KDN84225.1, ECO:0000313|Proteomes:UP000027178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN84225.1,
RC ECO:0000313|Proteomes:UP000027178};
RA Nam D.H.;
RT "Draft Genome Sequence of Kitasatospora cheerisanensis KCTC 2395.";
RL Submitted (MAY-2014) 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:KDN84225.1}.
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DR EMBL; JNBY01000093; KDN84225.1; -; Genomic_DNA.
DR RefSeq; WP_035864496.1; NZ_KK853997.1.
DR AlphaFoldDB; A0A066Z255; -.
DR PATRIC; fig|1348663.4.peg.3870; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_1_0_11; -.
DR Proteomes; UP000027178; 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:KDN84225.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027178}.
FT DOMAIN 64..333
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 40908 MW; 6052E9F71B703122 CRC64;
MTVMDHRDQS DPAVVPGWLP GATAPRTDPA PLLPDAEPFR VLGTPAADKA DPGLLRELYR
RLVAGRRYNQ QATTLTKQGR LAVYPASTGQ EACQVAAALA LRADDWMFPS YRDTLAVVAR
GVDPLQALTL LRGSAHTGYD PRATRTAPLC TPLATQVPHA VGLAHAARLA GDDTVALALL
GDGGTSEGDF HEGLNFAAVL HAPVVFLVQN NGYAISVPLT RQSAAPTLAH KAVGYGIPGR
LVDGNDAAAV HQVLTEAVER ARTGGGPTLV EALTYRVEAH TNADDATRYR HAEEVTAWQA
HDPIRLLEDA LRERGLLDEQ LVAEAADEAE AMAARMRAEF HADPDLDPMS LFAHVYAEPT
QQLREQAAQL AAELAAEAEV HAR
//