ID A0A1H3ZZB5_9FIRM Unreviewed; 484 AA.
AC A0A1H3ZZB5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Pyruvate dehydrogenase E2 component (Dihydrolipoamide acetyltransferase) {ECO:0000313|EMBL:SEA29219.1};
GN ORFNames=SAMN04515656_10730 {ECO:0000313|EMBL:SEA29219.1};
OS Eubacterium aggregans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=81409 {ECO:0000313|EMBL:SEA29219.1, ECO:0000313|Proteomes:UP000199394};
RN [1] {ECO:0000313|EMBL:SEA29219.1, ECO:0000313|Proteomes:UP000199394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR12 {ECO:0000313|EMBL:SEA29219.1,
RC ECO:0000313|Proteomes:UP000199394};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FNRK01000007; SEA29219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3ZZB5; -.
DR STRING; 81409.SAMN04515656_10730; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000199394; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 2.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF02817; E3_binding; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:SEA29219.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199394};
KW Transferase {ECO:0000313|EMBL:SEA29219.1}.
FT DOMAIN 36..73
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 52998 MW; B19A53994DC14B91 CRC64;
MERDDRRISR EERSRLRSIG EGHPAERVMA TGEPVRATPV ARRYAVEKGV DLADVAATMP
GRRIQPEDID RYLEQRQIFA KQKAYRSRIV PDDAGFLPDE QKVFKAVEEE MEKEEIIAKA
EAREAKLLQS TEPIPEPEKK DGEEASKENE ADDSVEAVEV AAPLAVPVIK ASPLAEAMAA
AEGIDLTLIE KGTGPDGCII KADITAYLNG LKPQYPDAHL VIFEPPALPA VIPVEPELAQ
EEVSEEVVLL PETGSELEPE AEPEAVASDT DRPEGQLNPP RVLTLTMEID LTELKETRKR
ITKRVEVQTG CRCTYTDFIL MAVAKALKLH PQLNGRFEGE AFVSKNQVHL GIGISNGDGL
AFPVIANVQN QSFGEVVKIR NGFLGDIKEQ GKLPEQKEAS TFDLVNLGVY GLLNATLPLA
EGLGAMLCIG DVVERYRYDQ GVGSNRPVVR ATLLLDSRIA GIGTAAGFLR DMKKELEHPT
AISF
//