ID A0A238VV30_HALVU Unreviewed; 552 AA.
AC A0A238VV30;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Pyruvate dehydrogenase E2 component (Dihydrolipoamide acetyltransferase) {ECO:0000313|EMBL:SNR38160.1};
GN ORFNames=SAMN06264855_104117 {ECO:0000313|EMBL:SNR38160.1};
OS Halorubrum vacuolatum (Natronobacterium vacuolatum).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=63740 {ECO:0000313|EMBL:SNR38160.1, ECO:0000313|Proteomes:UP000198397};
RN [1] {ECO:0000313|EMBL:SNR38160.1, ECO:0000313|Proteomes:UP000198397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8800 {ECO:0000313|EMBL:SNR38160.1,
RC ECO:0000313|Proteomes:UP000198397};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZNQ01000004; SNR38160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238VV30; -.
DR OrthoDB; 56234at2157; -.
DR Proteomes; UP000198397; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
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:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 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:SNR38160.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198397};
KW Transferase {ECO:0000313|EMBL:SNR38160.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 129..166
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 78..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 57736 MW; B7F635DA6DF9E032 CRC64;
MAIKEFKLPD VGEGVAEGEL VTWLVEPGDR VEEDQPVAEV ETDKALVEVP SRYDGVVEEL
FAEEGEIVPV GNVIISFRVD EDDEAPESAA DTDDGPAEPS EAEVDDTDVA DDTDAADDAD
AVAPGGRTFA PPSVRRLARE LGVDLAAVDG SGPGGRVGES DVRAYADEET DSADDEADDA
PTPKPIDIGS EDRGSAVTKR GGGDDSDAAA GGASAGATAT EPAGRDRTLA APATRKLARE
FGVEVDDVPT DRTREGEPFV DEAAVRAYAE ADASSAPPTD VTGAAEATDA AEAACTAGAT
AADPEGTVID RIPYRGVRRT IGKRMEQSKF TAPHVTHHDT AEVDALVDAR AELKPKAEAA
GVKLTYMPFV MKAVVAGLKA YPQLNSELRE EDEEILIKGE YNLGIAVATD AGLMVPVVRD
VDTKGLFELA DEVNDLAARA REREITPAEM KGGTFTLTNF GAIGGEYATP IINYPETAIL
GLGAIEERPV VRSHADVDGG FLDEADGSTV VPAPTLPLSL SIDHRVVDGA EAAAFANTVQ
DHLENPLLLL TE
//
