ID A0A0S7YPX2_9DELT Unreviewed; 226 AA.
AC A0A0S7YPX2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|ARBA:ARBA00016300};
DE AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|ARBA:ARBA00029730};
DE AltName: Full=E2 {ECO:0000256|ARBA:ARBA00031531};
DE Flags: Fragment;
GN ORFNames=AMJ54_12390 {ECO:0000313|EMBL:KPJ76265.1};
OS Deltaproteobacteria bacterium SG8_13.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703398 {ECO:0000313|EMBL:KPJ76265.1, ECO:0000313|Proteomes:UP000051346};
RN [1] {ECO:0000313|EMBL:KPJ76265.1, ECO:0000313|Proteomes:UP000051346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_13 {ECO:0000313|EMBL:KPJ76265.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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:KPJ76265.1}.
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DR EMBL; LJNK01000045; KPJ76265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7YPX2; -.
DR PATRIC; fig|1703398.3.peg.237; -.
DR Proteomes; UP000051346; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 134..171
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 88..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 226
FT /evidence="ECO:0000313|EMBL:KPJ76265.1"
SQ SEQUENCE 226 AA; 23449 MW; 98434D34D0541815 CRC64;
MARAFKLPDL GEGIHEGEVI TVLVSVGDEV KEGDPILEVE TDKAAVEIPS PYTGTVLEIM
VQPGQVVNVG DVLLTFSDGD KAAEKIETQT ASIEADKPTE TSPATAPAEA EVPPAAAPVV
TVNEAPADRK GPVPASPATR RLARELGVDL HRVTATGPGG LVTAEDVRTF AASGGERGLV
EIEETVVAVP LEGAGTAAAV PPLPDFSKWG PVKRMPLRSI RRATAR
//
