ID   A0A109IFW8_9ACTN        Unreviewed;       914 AA.
AC   A0A109IFW8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172, ECO:0000256|PIRNR:PIRNR000156};
DE            EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|PIRNR:PIRNR000156};
GN   ORFNames=GA0070623_5226 {ECO:0000313|EMBL:SCG80830.1};
OS   Micromonospora rifamycinica.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=291594 {ECO:0000313|EMBL:SCG80830.1, ECO:0000313|Proteomes:UP000198226};
RN   [1] {ECO:0000313|EMBL:SCG80830.1, ECO:0000313|Proteomes:UP000198226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44983 {ECO:0000313|EMBL:SCG80830.1,
RC   ECO:0000313|Proteomes:UP000198226};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that
CC       catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000256|PIRNR:PIRNR000156}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC         acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00043719,
CC         ECO:0000256|PIRNR:PIRNR000156};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000156-1};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964,
CC         ECO:0000256|PIRNR:PIRNR000156};
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DR   EMBL; LT607752; SCG80830.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109IFW8; -.
DR   OrthoDB; 9759664at2; -.
DR   Proteomes; UP000198226; Chromosome i.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR035807; PDC_E1_N.
DR   InterPro; IPR004660; PDH_E1.
DR   InterPro; IPR041621; PDH_E1_M.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005474; Transketolase_N.
DR   NCBIfam; TIGR00759; aceE; 1.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF3; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   Pfam; PF17831; PDH_E1_M; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000156-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000156};
KW   Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:SCG80830.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|PIRNR:PIRNR000156}.
FT   DOMAIN          148..311
FT                   /note="Transketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00456"
FT   DOMAIN          497..716
FT                   /note="Pyruvate dehydrogenase E1 component middle"
FT                   /evidence="ECO:0000259|Pfam:PF17831"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT   BINDING         274
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT   BINDING         276
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ   SEQUENCE   914 AA;  102043 MW;  F9B844A6D4169E9B CRC64;
     MATERKRPVI TAGLPSQLPD IDPEETGEWV ESLDGVIDER GTKRARYVML SLLERARERQ
     VGVPSLTTTD YINTIAPEQE PWFPGDEHIE RRIRAYVRWN AAMLVHRAQR PEIGVGGHIS
     TFASSASLYE VGFNHFFRGK NHPGGGDHIF YQGHASPGMY GRAFLEGRLS EDQLDGFRQE
     LSHPGGGLPS YPHPRLMPDF WEFPTVSMGL GPLNAIYQAR FNRYLQHRGI KDTSQQHVWA
     FLGDGEMDEV ESLGAIGVAA REELDNLTFV INCNLQRLDG PVRGNGKVMQ ELEAFFRGAG
     WNVIKVVWGR EWDPLLAADT DGALVNLMNT TPDGDYQTYK AESGAYVREH FFGRDQRTRK
     MVEHLSDDEI WNLKRGGHDY RKLYAAYKAA TEHTGQPTVI LAKTIKGWTL GSHFEGRNAT
     HQMKKLTLDD LKLFRDRLYL DIPDKALEEN PYLPPYYTPG ESSDELAYLR ERREQLGGYL
     PSRRTSHKKL AIPGSERFAD VKRGSGKQKV ATTMAFVRLL KDIMKDKEFG KRWVPIIPDE
     ARTFGLDSIF PTAKIYSPHG QRYTSVDRDL FLSYKESTTG QILHEGINEA GSVASFTAAG
     TSYATHDEPM IPMYIFYSMF GFQRTGDGFW AAADQMARGF VLGATAGRTT LNGEGLQHED
     GHSLLLAATN PAVVAYDAAF GFELAHIVER GLHRMYGEDQ ENIFYYLTVY NEPIHQPVEP
     SELDVEGLLR GIYRYAGAPQ VDGDAPKANI LASGTGMQWA LKAQQLLAQD WGVAADVWSV
     TSWTELRRDA VLCEEHNLLN PGAEQRVPYI QEKLADADGP KVAVSDWMRA VPDLISRWVP
     GDYTSLGTDG FGMSDTRHAL RRHFHVDAES VAVATLRQLA LRGAVPATVP AEAAKKYAID
     DVNSAPVGET GGDS
//