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Database: UniProt
Entry: A0A2A5QZG9_9EURY
LinkDB: A0A2A5QZG9_9EURY
Original site: A0A2A5QZG9_9EURY 
ID   A0A2A5QZG9_9EURY        Unreviewed;       552 AA.
AC   A0A2A5QZG9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Branched-chain alpha-keto acid dehydrogenase subunit E2 {ECO:0000313|EMBL:PCR92227.1};
GN   ORFNames=CP557_17835 {ECO:0000313|EMBL:PCR92227.1};
OS   Natrinema ejinorense.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=373386 {ECO:0000313|EMBL:PCR92227.1, ECO:0000313|Proteomes:UP000219689};
RN   [1] {ECO:0000313|EMBL:PCR92227.1, ECO:0000313|Proteomes:UP000219689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13890 {ECO:0000313|EMBL:PCR92227.1,
RC   ECO:0000313|Proteomes:UP000219689};
RA   Roh S.W., Kim Y.B., Kim J.Y.;
RT   "Genome sequences of Natrinema ejinorence JCM 13890T.";
RL   Submitted (SEP-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}.
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:PCR92227.1}.
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DR   EMBL; NXNI01000001; PCR92227.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5QZG9; -.
DR   OrthoDB; 56234at2157; -.
DR   Proteomes; UP000219689; 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;
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          137..174
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          80..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  58506 MW;  02595C7F13AF31A1 CRC64;
     MVREFELPDV GEGVAEGELV SWLVEAGDEV TEDQPVAEVE TDKALVEVPA PVDGTVRELH
     VEEGEVVPVG TVIISFDVEG EESEAPRASE NANGEAVSEG AAAPTESEQE TTSEPAGDPG
     ATGADTEAVA PPDDRVFAPP RVRRMAREEG VDLSRIQGSG PGGRITAADV QAATGDSSGE
     PAGSQSQSAG AAASEAASGT ADSTGRSAGA SAAEETTPED ATASSSTGRP ETPTRVESAD
     RERTLAAPAT RRIAQEEGVD IDAVPATEER DGEAFVTPEA IQEYADAQRQ AQEADREAVE
     AGESVGTKGA QFAEGERERR EPFTGVRKTI ADAMVESKYS APHVTHHDEV DVTELVAARE
     DLKPRAEERG IRLTYMPFIM KAVVAALKEY PEMNAVIDEE NEEIVYRDYY NIGVATATDV
     GLMVPVVEDA DRKGLLQLSS EMNEVVQKAR DRTISPDELR GSTFTITNVG GIGGEYATPI
     INYPEAGILA IGEIKRKPRV VTDENGSESI EPRSVLTLSL SFDHRLIDGA VGAAFTNTVM
     EYLENPSLLL LE
//
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