ID H0AF37_HALSG Unreviewed; 200 AA.
AC H0AF37;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Branched-chain alpha-keto acid dehydrogenase subunit E2 {ECO:0000313|EMBL:EHK00607.1};
GN ORFNames=HRED_00900 {ECO:0000313|EMBL:EHK00607.1};
OS Haloredivivus sp. (strain G17).
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Nanohaloarchaea;
OC Candidatus Haloredivivus.
OX NCBI_TaxID=1072681 {ECO:0000313|EMBL:EHK00607.1, ECO:0000313|Proteomes:UP000003484};
RN [1] {ECO:0000313|EMBL:EHK00607.1, ECO:0000313|Proteomes:UP000003484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G17 {ECO:0000313|EMBL:EHK00607.1,
RC ECO:0000313|Proteomes:UP000003484};
RA Ghai R., Pasic L., Fernandez A.B., Martin-Cuadrado A.-B., Mizuno C.M.,
RA McMahon K.D., Papke R.T., Stepanauskas R., Rodriguez-Brito B., Rohwer F.,
RA Sanchez-Porro C., Ventosa A., Rodriguez-Valera F.;
RT "New Dominant Microbial Groups Along A Salinity Gradient.";
RL Sci. Rep. 0:0-0(2011).
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:EHK00607.1}.
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DR EMBL; AGNT01000416; EHK00607.1; -; Genomic_DNA.
DR AlphaFoldDB; H0AF37; -.
DR Proteomes; UP000003484; 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:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000003484}.
FT DOMAIN 1..75
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 149..183
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 75..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 200 AA; 21378 MW; CC9CB621D0FC4734 CRC64;
MKFKFPDTGE GVTEGQFLEW KVEEGEEVEE DQIVGEAETD KAVVDIPAPA DGIVKELKAS
PGDNVKVGDV IMILNTDADS SGKETSNDSE DSEKAGESKV DGQEASKNDS KKDAVMGGSP
SKSSYDHDEG QKEETDNKEA SEPSSSDVLA LPKVRKLAEK KGLNLASLDI DGRITEEDVL
EASKSGEVKE SEAEPEDEEG
//
