ID A0A1G6S2V8_9MICO Unreviewed; 914 AA.
AC A0A1G6S2V8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05216410_2862 {ECO:0000313|EMBL:SDD11240.1};
OS Sanguibacter gelidistatuariae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC Sanguibacter.
OX NCBI_TaxID=1814289 {ECO:0000313|EMBL:SDD11240.1, ECO:0000313|Proteomes:UP000199039};
RN [1] {ECO:0000313|EMBL:SDD11240.1, ECO:0000313|Proteomes:UP000199039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISLP-3 {ECO:0000313|EMBL:SDD11240.1,
RC ECO:0000313|Proteomes:UP000199039};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-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; FMYH01000005; SDD11240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6S2V8; -.
DR STRING; 1814289.SAMN05216410_2862; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000199039; Unassembled WGS sequence.
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:SDD11240.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199039};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 149..311
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 502..718
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; 100818 MW; BD27A393F04E60E8 CRC64;
MATHDETGPL INGLLSQVPD IDPSETGEWV ESLDGLIDDR GGPRARYVLL NLLKRARERN
VAIPTSINTP YVNTIGVHEE PYFPGDEVIE RRYRSWNRWN AAVMVTRAQR PGIGVGGHIS
SYASVATLYE VGLNHFFHGK DHPGGGDQVY FQGHASPGVY SRAFLEGRLS AEDLDGFRQE
HSHAGGGLPS YPHPRQMRDF WEFPTVSMGL GPASAIYQAW TNRYLNNRGI KDTSQQNVWA
FLGDGEMDEP ESRGMLQLAA QQQLDNLTFV VNCNLQRLDG PVRGNGKIIQ ELEAQFKGAG
WNVIKVIWGR EWDVLLNADK DRSLVNLMNE TPDGDYQTYR AEDGAFIREH FFGRDPRTKQ
LVENLSDDDI WALKRGGHDY RKIYAAYAAA MAHTGQPTVI LAHTIKGYGL GSGFAGRNST
HQMKKVGPAD LKTLRDTLHI PITDAELDAD PYAPPYYHPG VDAPEIQYML DRRAKLGGFV
PERRSVSTAV TLPADSKYDI LKKGSGAQEI ATTQAFVRLL KDLIKDKEFG NRIVPIIPDE
ARTFGLDSIF PSAKIFNTLG QNYLAVDRDL MLSYKESESG QIMHTGINEA GSASAFQAVG
TSYATHGEVM IPFYIFYSMF GFQRTGDQFW AAGDQLTRGF IIGATAGRTT LTGEGLQHAD
GHSPILAATN AAIVQYDPAY GYEISHIVRD GIQRMYGENE SRDPNVMYYL TVYNEPMTQP
AEPADVDADG ILRGIHRIAA SDAEGPKAQI LASGVGVPWA IEAKELLAKD WGVQADVWSV
TSWNELRRDG LAAEQHNFLH PSEPEREAYL TTKLKDAQGP FVATSDFDHL VPDQVRQWIP
GEYAVLGADG FGFSDTRAAA RRYFKIDGPS VVVRVLQQLA RRGEVAADAP ARAIEQYQLH
DVNAGASGNA GGAS
//
