ID A0A1B8NW99_HALEL Unreviewed; 892 AA.
AC A0A1B8NW99;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 Name=aceE {ECO:0000313|EMBL:OBX34262.1};
GN ORFNames=A8U91_03315 {ECO:0000313|EMBL:OBX34262.1}, DKQ62_00025
GN {ECO:0000313|EMBL:RAW08985.1};
OS Halomonas elongata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=2746 {ECO:0000313|EMBL:OBX34262.1, ECO:0000313|Proteomes:UP000092504};
RN [1] {ECO:0000313|EMBL:OBX34262.1, ECO:0000313|Proteomes:UP000092504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HEK1 {ECO:0000313|EMBL:OBX34262.1,
RC ECO:0000313|Proteomes:UP000092504};
RA Gaba S., Singh R.N., Abrol S., Kaushik R., Saxena A.K.;
RT "Genome sequence of halotolerant plant growth promoting strain of Halomonas
RT elongata HEK1 isolated from salterns of Rann of Kutch, Gujarat, India.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAW08985.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH25661 {ECO:0000313|EMBL:RAW08985.1};
RA Mamani I.J., Pacheco K.B., Quispe-Ricalde M.A.;
RT "Draft genome sequence of Halomonas elongata strain MH25661 isolated of
RT saline creek in the Andes from Peru.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000251811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH25661 {ECO:0000313|Proteomes:UP000251811};
RX PubMed=30637380; DOI=10.1128/mra.00934-18;
RA Mamani J.I., Pacheco K.B., Elorrieta P., Romoacca P., Castelan H.,
RA Davila S., Sierra J.L., Quispe-Ricalde M.A.;
RT "Draft Genome Sequence of Halomonas elongata MH25661 Isolated from a Saline
RT Creek in the Andes of Peru.";
RL Microbiol. Resour. Announc. 8:0-0(2019).
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: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};
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:OBX34262.1}.
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DR EMBL; MAJD01000002; OBX34262.1; -; Genomic_DNA.
DR EMBL; QJUB01000001; RAW08985.1; -; Genomic_DNA.
DR RefSeq; WP_013333328.1; NZ_QJUB01000001.1.
DR AlphaFoldDB; A0A1B8NW99; -.
DR PATRIC; fig|2746.7.peg.3408; -.
DR OMA; PDEYRTF; -.
DR Proteomes; UP000092504; Unassembled WGS sequence.
DR Proteomes; UP000251811; 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; 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:OBX34262.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 100..293
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 476..704
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 892 AA; 100946 MW; EF3E62649EA6FA90 CRC64;
MSLETREDLD PVETQEWLDS LESVLDREGE DRARYLMNRL ADRYRRDGMQ VPFSVTTPHR
NTIPVHREAP MPGDLFMERR IRSLIRWNMA AMVTRANKAN KGIGGHLASF MSSATLYDVG
FNHFFRAANG DFKGDLVFIQ GHSSPGVYAR AFLEGRLTEE QMDKFRQEVD GDGLSSYPHP
WLMPDFWQLP TVSMGLGPIM AIYQAHVMKY LDQRGLQPMQ DRKVWAFLGD GECDEPETLG
AIHLASREKL DNLNFVVNCN LQRLDGPVRG NSRIMDELEG VFRGAGWNVI KVVWGRLWDP
LFEKDKKGIL QKRMDEAVDG EYQNYKANGG AYTREHFFGK YPETAELVKD MSDEDIWKLN
RGGHDPFKIY AAYHEAFHNT SGRPTVILAH TVKGYGLGAA GGEADNEAHQ VKSIDDPDVL
KDFRDRFGIP VSDEQIENEM PYYKPDDDSP EMKYMHLQRE RLGGYLPARN PDFEALEIPS
LEDKTFASQL KGSNGREVST TMAFVRILNG LVKDKKVGKQ VVPIVPDEAR TFGMEGMFRQ
LGIYTSEGQK YEPMDKGQLM FYREDQAGQV LEEGITEAGA MSSWIAAATS YSNHGLPLLP
FYIYYSMFGF QRIGDLAWAA GDMQARGFLV GGTAGRTTLN GEGLQHQDGH SHLQASMIPN
CRSYDPTYAH EVAVIVQDGL KRMYADKENC FYYLTVMNEN YEQPALEEVP TEDIIKGMYL
LRETQGDKAR VQLMGSGTIL REVEEAAELL AEEWGIGADI WSVTSFNELR REALEIDRQA
FLKPAEEPGK PHVTACLEGR QGPAIASTDY MKLFADQVRA WVPTDYHVLG TDGYGRSDTR
EKLRHFFEVD RYFVTVTALK ALADRGEIDR KVVAEAIEKY GIDPNKPNPL EV
//
