ID A0A0X3UV43_9ACTN Unreviewed; 391 AA.
AC A0A0X3UV43;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) E1 component subunit alpha {ECO:0000313|EMBL:KUL35977.1};
GN ORFNames=ADL22_25745 {ECO:0000313|EMBL:KUL35977.1};
OS Streptomyces sp. NRRL F-4489.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL35977.1, ECO:0000313|Proteomes:UP000053256};
RN [1] {ECO:0000313|EMBL:KUL35977.1, ECO:0000313|Proteomes:UP000053256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL35977.1,
RC ECO:0000313|Proteomes:UP000053256};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL35977.1}.
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DR EMBL; LLZI01000254; KUL35977.1; -; Genomic_DNA.
DR RefSeq; WP_066984506.1; NZ_LLZI01000254.1.
DR AlphaFoldDB; A0A0X3UV43; -.
DR STRING; 1609095.ADL22_25745; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000053256; 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:KUL35977.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053256}.
FT DOMAIN 71..330
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 42274 MW; A4D9F6FA4903EE00 CRC64;
MTVLEQPGSP RHTSGPAGPP PAWRPRVDPA PLLPDAEPYR LLGTDAARRL DTGLLKRLYA
ELVRGRRYNT QATALTRQGR LAVYPSSTGQ EACQVAAALA LQEQDWLFPS YRDTLAAVAR
GLDPVQALTL LRGDWHTGYD PYEHRVAPLC TPLATQLPHA VGLAHAARLK GDDVVALAMV
GDGGTSEGDF HEALNFAAVW QAPVVFLVQN NGFAISVPLA KQTAAPSLAH KAVGYGMPGR
LVDGNDAPAM HEVLTDAVRR AREGGGPTLV EAVTYRLDAH TNADDATRYR TEAEVETWRA
HDPIALMERE LTDRGLLTDA FAAATRESAE QLAAALRDRM HTDPPLDPMA LFDHVFARQT
GQLRDQADRL RAELDAEAEA ATPAPAQEAR P
//
