ID   A0A0M4MDZ7_9MICC        Unreviewed;       364 AA.
AC   A0A0M4MDZ7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:ALE07642.1};
GN   ORFNames=AL755_07105 {ECO:0000313|EMBL:ALE07642.1};
OS   Arthrobacter sp. ERGS1:01.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE07642.1, ECO:0000313|Proteomes:UP000060433};
RN   [1] {ECO:0000313|EMBL:ALE07642.1, ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE07642.1,
RC   ECO:0000313|Proteomes:UP000060433};
RX   PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA   Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT   "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT   bacterium with prospective cold active industrial enzymes, isolated from
RT   East Rathong glacier in India.";
RL   J. Biotechnol. 214:139-140(2015).
RN   [2] {ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA   Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT   "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL   Submitted (AUG-2015) 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; CP012479; ALE07642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M4MDZ7; -.
DR   STRING; 1704044.AL755_07105; -.
DR   KEGG; are:AL755_07105; -.
DR   PATRIC; fig|1704044.3.peg.644; -.
DR   Proteomes; UP000060433; Chromosome.
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:ALE07642.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060433}.
FT   DOMAIN          36..304
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   364 AA;  39104 MW;  990D904B74FFD3D4 CRC64;
     MHQLIAADGT AVTDALLAPL VADVDDAQLL DLYSDMVVIR RIDFEATALQ RQGQLALWPP
     MLGQEAAQIG SVRALEKDDF IFPTYRENGV AYCRGAKLAG IMSTWRGSAN TGWDPYEFNM
     ATPQIIIGAQ TLHAAGYAMG LTMDGKESLA IAYLGDGATS QGDVHESMVF AASFQAPVIF
     FCQNNHWAIS EPVRLQSHVP LAGRAAGYGI PGLRVDGNDV LAVLAATRWA AARARSGAGP
     SFIEAVTYRM GPHTTADDPT RYRGVTELEE WAAKDPIARV RAFLLGRGAL DDAGEAAVAA
     RADAVAAELR EGTINMPDPD PMTVFDNVYT SEHSILDRQR EHYARYLAGF AGASDTATLE
     GNRS
//