ID   A0A243RZL9_9ACTN        Unreviewed;       381 AA.
AC   A0A243RZL9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) E1 component subunit alpha {ECO:0000313|EMBL:OUD00615.1};
GN   ORFNames=CA983_24605 {ECO:0000313|EMBL:OUD00615.1};
OS   Streptomyces swartbergensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=487165 {ECO:0000313|EMBL:OUD00615.1, ECO:0000313|Proteomes:UP000195105};
RN   [1] {ECO:0000313|EMBL:OUD00615.1, ECO:0000313|Proteomes:UP000195105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMC13 {ECO:0000313|EMBL:OUD00615.1};
RA   Le Roes-Hill M., Prins A., Durrell K.A.;
RT   "Biotechnological potential of actinobacteria isolated from South African
RT   environments.";
RL   Submitted (MAY-2017) 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:OUD00615.1}.
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DR   EMBL; NGFN01000166; OUD00615.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A243RZL9; -.
DR   Proteomes; UP000195105; 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:OUD00615.1}.
FT   DOMAIN          64..342
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          357..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   381 AA;  41337 MW;  9272ED487609923B CRC64;
     MTVMEQRGAY RPTPPPAWQP RTDPAPLLPD AEPYRVLGTE AAAQADPELL RTLYAQLVRG
     RRYNAQATAL TKQGRLAVYP STTGQEACEI AAALVLEERD WLFPSYRDTL AVVARGVDPV
     EALTLLRGDW HTGYDPYEHR VAPLCTPLAT QLPHAVGLAH AARLRGDDVV ALAMVGDGGT
     SEGDFHEALN FAAVWQAPVV FLVQNNGFAI SVPIAKQTAA PSLAHKAVGY GMPGRLVDGN
     DAVAVHEVLS DAVRHARAGG GPTLVEAITY RVDAHTNADD ATRYRGDAEV EAWREHDPIQ
     LLERELTARG LLDEAGKQAA RDAAEAMAAD LREHMNQDPV LDPMDLFAHV YAEPTSQLRD
     QREQLRAELE AEAGPEGGTH R
//