ID A1UJ85_MYCSK Unreviewed; 356 AA.
AC A1UJ85;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) {ECO:0000313|EMBL:ABL92893.1};
DE EC=1.2.4.1 {ECO:0000313|EMBL:ABL92893.1};
GN OrderedLocusNames=Mkms_3699 {ECO:0000313|EMBL:ABL92893.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL92893.1};
RN [1] {ECO:0000313|EMBL:ABL92893.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL92893.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP000518; ABL92893.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UJ85; -.
DR STRING; 189918.Mkms_3699; -.
DR KEGG; mkm:Mkms_3699; -.
DR HOGENOM; CLU_029393_1_0_11; -.
DR OrthoDB; 9766715at2; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:ABL92893.1}; Pyruvate {ECO:0000313|EMBL:ABL92893.1}.
FT DOMAIN 37..322
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 356 AA; 38854 MW; 8A0AFC1D0A27F725 CRC64;
MAGVELDPVQ LVGADGSPSA QQRYSRDLPP ETLAWLYETM VVTRDLDTEF VHLQRQGELA
LYASCRGQEA AQIGATACLR KTDWLFPQYR EIGAFLLRGI APAQMAAVWR GKWHGGLEFT
AKCCAPISIP IGTQGLHAVG AAMAAQRLGE DSVTVAFLGD GATSEGDVHE AMNLAAVYQV
PCVFFVQNNQ WAISVPVQRQ VAGPSIAHRA AGYGMPGVRV DGNDVLACFA VMSEAAARAR
AGGGPTLIEA VTYRLGPHTT SDDPTRYRDQ SEVDRWRARD PIPRYRTYLQ GAGVWSERLE
ERVAARSKRL RAELRDAVVG APDFDVSEVF DTVYHDITPD LAEQRDRLLA ELAKEA
//
