ID A0A1G5ICB6_9ACTN Unreviewed; 382 AA.
AC A0A1G5ICB6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Pyruvate dehydrogenase E1 component alpha subunit {ECO:0000313|EMBL:SCY73643.1};
GN ORFNames=SAMN02745898_103242 {ECO:0000313|EMBL:SCY73643.1};
OS Streptomyces sp. 136MFCol5.1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1172182 {ECO:0000313|EMBL:SCY73643.1, ECO:0000313|Proteomes:UP000199326};
RN [1] {ECO:0000313|EMBL:SCY73643.1, ECO:0000313|Proteomes:UP000199326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=136MFCol5.1 {ECO:0000313|EMBL:SCY73643.1,
RC ECO:0000313|Proteomes:UP000199326};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FMVI01000003; SCY73643.1; -; Genomic_DNA.
DR RefSeq; WP_030930283.1; NZ_FMVI01000003.1.
DR AlphaFoldDB; A0A1G5ICB6; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000199326; 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:SCY73643.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199326}.
FT DOMAIN 61..341
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 42310 MW; 603DD2DDE257D348 CRC64;
MTVESTAARK PRRSSKRTSA AKTPQSSEPE LVQLLTPEGE RVEHPDYEID LTADELRGLY
RDMVLTRRFD AEATALQRQG ELGLWASLLG QEAAQIGSGR ALRDDDYVFP TYREHGVAWC
RGVDPTNLLG MFRGVNHGGW DPNTNNFHLY TIVIGSQTLH ATGYAMGVAK DGADSAVIAY
FGDGASSQGD VAEAFTFSAV YNAPVVFFCQ NNQWAISEPT EKQTRVPLYQ RAQGFGFPGV
RVDGNDVLAC LAVTKSALER ARRGEGPTLV EAFTYRMGAH TTSDDPTKYR ADEERVSWEA
KDPILRLRTY LEQQELADEA FFTALDEESE ALGKRVREAV RAMPDPDRMA IFDHAYADGN
PLVDEERAQF AAYQASFAEE GN
//