ID A0A1I2WIH3_9EURY Unreviewed; 530 AA.
AC A0A1I2WIH3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Pyruvate dehydrogenase E2 component (Dihydrolipoamide acetyltransferase) {ECO:0000313|EMBL:SFH01112.1};
GN ORFNames=SAMN04488063_3580 {ECO:0000313|EMBL:SFH01112.1};
OS Halopelagius inordinatus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=553467 {ECO:0000313|EMBL:SFH01112.1, ECO:0000313|Proteomes:UP000198876};
RN [1] {ECO:0000313|Proteomes:UP000198876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7739 {ECO:0000313|Proteomes:UP000198876};
RA Varghese N., Submissions S.;
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; FOOQ01000008; SFH01112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2WIH3; -.
DR STRING; 553467.SAMN04488063_3580; -.
DR OrthoDB; 56234at2157; -.
DR Proteomes; UP000198876; 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; 2.
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:SFH01112.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198876};
KW Transferase {ECO:0000313|EMBL:SFH01112.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 123..160
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 80..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..112
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 55859 MW; 7D1D898C9727DFD9 CRC64;
MGIKEFKLPD VGEGVAEGEL VTWHVSPGDT VTEDQVVAEV ETDKALVDVP SPYNGTVSEL
RAEEGEMVPV GDVIITFEVE GEGDEPADAE VQTETEADDS DADEEPEEET APSETESPSG
RVFAPPSVRR LARELGVDLA SVSGSGPSGR VTEGDVRSAA EGADAGGDGE SGGPRSVSFS
GNSAVSKAGD SGNGQDAGSA DSSAPAPQAA GREKTLAAPA TRRIAEEEGV SIDDVPATEK
RDGEPFVTEA DVRQYAEVQR EAQRADAESV SAEAGAGEAS ETADLPAQTV EPEADAGPGA
GERVPYKGVR KAIGDQMQRS KYTAPHVTHH DEVDVTELVE LREEFKPMAG ERDVKLTYMP
FVTKAVVAAL KQFPYMNAQL DEENEEIVLR DEYNVGVATA TDAGLLVPVV HGADGKGLLD
LARETNELVE KARSRKISPA EMQGGTFTIT NVGVIGGEYA TPIINYPEVG ILALGAIKEK
PRVVDGEIVP RKVLTLSLSF DHRVVDGAIA ARFTNKVGEY LSNPKLLLLE
//
