ID F2NQ56_MARHT Unreviewed; 900 AA.
AC F2NQ56;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 OrderedLocusNames=Marky_0617 {ECO:0000313|EMBL:AEB11367.1};
OS Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Marinithermus.
OX NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB11367.1, ECO:0000313|Proteomes:UP000007030};
RN [1] {ECO:0000313|EMBL:AEB11367.1, ECO:0000313|Proteomes:UP000007030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030};
RX PubMed=22675595; DOI=10.4056/sigs.2435521;
RA Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S.,
RA Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Pan C., Brambilla E.M., Rohde M., Tindall B.J., Sikorski J.,
RA Goker M., Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the aerobic, heterotroph Marinithermus
RT hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent
RT chimney.";
RL Stand. Genomic Sci. 6:21-30(2012).
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; CP002630; AEB11367.1; -; Genomic_DNA.
DR AlphaFoldDB; F2NQ56; -.
DR STRING; 869210.Marky_0617; -.
DR KEGG; mhd:Marky_0617; -.
DR eggNOG; COG2609; Bacteria.
DR HOGENOM; CLU_009154_2_0_0; -.
DR Proteomes; UP000007030; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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}; Pyruvate {ECO:0000256|PIRNR:PIRNR000156};
KW Reference proteome {ECO:0000313|Proteomes:UP000007030};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 88..303
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 492..708
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 900 AA; 100831 MW; DF6C6CF2C60C1941 CRC64;
MIARRAALSP EEQRLLERIE DQEWLESLEY VLESAGPERT RALLELLERH ALRHGVALPF
VGNTPLTNTI PAEQEMPYPG DLELEARIRN LIRWNAVAMV VRANKHSDGI GGHLATYASA
AELFEVGFNH FFRGREKGFD RDLVYIQGHA SPGIYARAFL EGRLSEAQLR NFRRELKPEG
GLASYPHPWL MPEFWEYPTV SMGLGPIMSI YQARFMRYLE HRGLKPKSSA KVWAFIGDGE
TDEPEILGAL RVAARERLDN LIWVVNCNLQ RLDGPVYGNG QVVQELERIF RGAGWNVIKV
AWGRRWDALL ARDTEGRLLK RFAETVDGWW QKYVAEGPRF FREHFFGADP KLAELVQDLS
DADLEALLRD RGGHDPTKVY AAYRAAVEHR GQPTVILAHT IKGYGLGAVA EARNVAHQVK
KLDTSALREF RDRLQIPVPD EALEEVPFYR PDPDSPEIRY LRERRAALGG FVPKREVKAE
PLPVPEEAFF EEFYKGTGGR PVSTTMALVR IIAKLLRHKE LGRRVVPIIP DEGRTFGMEA
LVAQVGIYSP VGQRYEPPDA GSLLVYKEAQ DGQILEEGIT EAGAMSSFIA AGTAHTNYGI
PMIPFYIYYS MFGFQRVGDL IWAAGDSRAR GFLIGATAGR TTLAGEGLQH QDGHSHVAAL
TVPNLVAYDP AFAYEIAVII QDGLRRMYHE GEDVFYYITV GNENYAQPEM PEPRETVKEG
ILKGLYKLRA SNLADAKHRA QLFGSGAILN EVLKAQELLE AYGVAADVWS VTSYKNLYRD
AVETDRWNRL HPTEAPRLPY AAQVLKDAPG VFVAASDYMK LLPDALSGYL PKRMHALGTD
GFGRSEARAE LRDHFEVDAR HITVATLAAL AREGELDPKV VEQAIQKLGV DPEKPDPVKL
//
