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Entry: A0A063Y5B8_9GAMM
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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
//
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