ID A0A022MC29_9ACTN Unreviewed; 408 AA.
AC A0A022MC29;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:EYT80076.1};
GN ORFNames=CF54_27530 {ECO:0000313|EMBL:EYT80076.1};
OS Streptomyces sp. Tu 6176.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1470557 {ECO:0000313|EMBL:EYT80076.1, ECO:0000313|Proteomes:UP000020060};
RN [1] {ECO:0000313|EMBL:EYT80076.1, ECO:0000313|Proteomes:UP000020060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu 6176 {ECO:0000313|EMBL:EYT80076.1,
RC ECO:0000313|Proteomes:UP000020060};
RA Olano C., Cano-Prieto C., Mendez C., Salas J.A.;
RT "Draft genome sequence of Streptomyces sp. Tu 6176, producer of the
RT cytotoxic benzoxazol nataxazol.";
RL Submitted (MAR-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:EYT80076.1}.
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DR EMBL; JFJQ01000889; EYT80076.1; -; Genomic_DNA.
DR RefSeq; WP_018569127.1; NZ_KK106991.1.
DR AlphaFoldDB; A0A022MC29; -.
DR HOGENOM; CLU_029393_1_0_11; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000020060; 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:EYT80076.1}.
FT DOMAIN 86..367
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 408 AA; 44334 MW; C5911EC6685FB8C4 CRC64;
MTVESTAART SRRSAGSKAG TSGTKAAGTT GTKGTTRTTA RKAAAAKGAE PGLVQLLTPE
GKRVKNAEYD KYVSGITADD LRGLYRDMVL TRRFDAEATA LQRQGELGLW ASLLGQEAAQ
IGSGRALRDD DYVFPTYREH GVAWCRGVDP TNLLGMFRGV NNGGWDPNGN NFHLYTIVIG
SQTLHATGYA MGIAKDGADS AVIAYFGDGA SSQGDVAESF TFSAVYNAPV VFFCQNNQWA
ISEPTEKQTR VPLYQRAQGY GFPGVRVDGN DVLATLAVTR WALERARAGE GPTLVEAYTY
RMGAHTTSDD PTRYRHDDER AAWEAKDPIL RLRRHLEASH HADEGFFAEL DAESETLGKR
VREAVRAMPD PDHFAIFENV YADGHALVDE ERAQFAAYQA SFADAEGV
//
