ID A0A1H7LJ90_9RHOB Unreviewed; 394 AA.
AC A0A1H7LJ90;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Pyruvate dehydrogenase E2 component (Dihydrolipoamide acetyltransferase) {ECO:0000313|EMBL:SEK99042.1};
GN ORFNames=SAMN04488526_1745 {ECO:0000313|EMBL:SEK99042.1};
OS Jannaschia helgolandensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=188906 {ECO:0000313|EMBL:SEK99042.1, ECO:0000313|Proteomes:UP000199283};
RN [1] {ECO:0000313|EMBL:SEK99042.1, ECO:0000313|Proteomes:UP000199283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14858 {ECO:0000313|EMBL:SEK99042.1,
RC ECO:0000313|Proteomes:UP000199283};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00043782};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNZQ01000002; SEK99042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7LJ90; -.
DR STRING; 188906.SAMN04488526_1745; -.
DR OrthoDB; 9804723at2; -.
DR Proteomes; UP000199283; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:SEK99042.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199283};
KW Transferase {ECO:0000313|EMBL:SEK99042.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 121..158
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 78..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 40590 MW; 78466A198800883F CRC64;
MGRVILTLPR LGETMEEAKV TEWLVVIGAV YARGDVLLEV ETDKTVVEVP ALAAGTLLKQ
LVAPGDMVEL DAPIAEVEQE GDVSVAGPEP TAPIPTADMP APTKPAPTPP SAPRDASGRI
AASPAARAEA RRRGVSLSGM SGSGRRGRIT ADDVGGDDDG TVVLIHGLFD NSTGWRGLPQ
RLARRGLACI TLDLPGHGTD TTSADTFDQA AALLADRLPI GPLHLVGHSL GAALAARLAT
RIGARARSLT LFAPAGLGAA ISADFLTGMA QASSAEALKT VLALLDGGPI SDAAIAQQLP
QHLAGLAVRS RLAEAVARDG RQQIDATADI AAAPCPVTVV FGTADRILDW RDVAHLPAET
RIHLIPNAGH LPHLVRPDLA AALIAPRHDP AETA
//
