ID A0A063Y5B8_9GAMM Unreviewed; 878 AA.
AC A0A063Y5B8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=ADINL_0523 {ECO:0000313|EMBL:KDE40874.1};
OS Nitrincola lacisaponensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=267850 {ECO:0000313|EMBL:KDE40874.1, ECO:0000313|Proteomes:UP000027318};
RN [1] {ECO:0000313|EMBL:KDE40874.1, ECO:0000313|Proteomes:UP000027318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4CA {ECO:0000313|EMBL:KDE40874.1,
RC ECO:0000313|Proteomes:UP000027318};
RX PubMed=16280482; DOI=10.1099/ijs.0.63647-0;
RA Dimitriu P.A., Shukla S.K., Conradt J., Marquez M.C., Ventosa A.,
RA Maglia A., Peyton B.M., Pinkart H.C., Mormile M.R.;
RT "Nitrincola lacisaponensis gen. nov., sp. nov., a novel alkaliphilic
RT bacterium isolated from an alkaline, saline lake.";
RL Int. J. Syst. Evol. Microbiol. 55:2273-2278(2005).
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|ARBA:ARBA00003157, 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:ARBA00033635,
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDE40874.1}.
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DR EMBL; JMSZ01000015; KDE40874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A063Y5B8; -.
DR STRING; 267850.ADINL_0523; -.
DR PATRIC; fig|267850.7.peg.517; -.
DR Proteomes; UP000027318; Unassembled WGS sequence.
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; IPR001849; PH_domain.
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.
DR PROSITE; PS50003; PH_DOMAIN; 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:KDE40874.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027318};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 1..18
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 878 AA; 99847 MW; 85930F61EDD6E502 CRC64;
MDPVETQEWL EALESVAKHE GDDRARYILQ KLGNKASEIG LGAAGSLTTP YRNTIAPKDE
ARMPGDLFME RRIRSFIRWN AMAMVMRANS NSDALGGHIS SFSSSATLYD IGFNYFFHGP
EGDRESDMVF FQGHISPGIY ARAYLEGRLT EEQMDNFRRE VDGNGLSSYP HPWLMPDFWQ
FPTVSMGLGP IQAIYQAHVM RYLSARELIK RGNRKVWAFL GDGECDEPES LGAISLAGRE
QLENLVFVVN CNLQRLDGPV RGNGKIVQEL ESIFRGAGWN VIKCLWGRHW DPLFDKDDKG
LLQKRMDEVC DGELQNYKAN GGAYTREHFF GKYPELLEMV SDMSDQDIMN LNRGGHDPYK
VYAAYHAAMN HKGQPTVILA QTVKGYGTGQ SGEAKNDTHS MKKVALDDLK AFRDRFNIPL
DDEQLESVPY YRPSPDSPEM KYMFERRKQL GGFYPARRNS FDKLETPELE VFSSQLKGTG
EREISTQMAL NRVLSTLVKD KNIGNRIVPI VPDEARTFGM EGMFRQLGIY TSQGQRYTPH
DRDQIMYYKE SKTGQILEEG INESGAFSAW LACATSYSNN NCPVIPFYIF YSMFGFQRVM
DLTWAAGDSQ ARGFLIGATS GRTTLNGEGL QHQDGHSHLM AQMIPNCVSY DPTYGYELTV
IIQDGLKRMF QDQENKFYYI TTLNENYQHP DMPAGAEEGI IKGMYLLEEG KKADLRVQLM
GCGSILREVR EAAEILRNEF GVEADVWSTT SINELRRDAQ AVYRWNMLHP EEQPRESYIE
QALKGHEGPV IASTDYMRMF ADQLREYIPR RYKVLGTDGF GRSDSRAKLR EFFEVNRYYV
VVAALKALQE EGKLEAAVVA KAMQKFHINP EKPAPWTV
//