ID M0CE71_9EURY Unreviewed; 560 AA.
AC M0CE71;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Branched-chain alpha-keto acid dehydrogenase subunit E2 {ECO:0000313|EMBL:ELZ21556.1};
GN ORFNames=C477_05741 {ECO:0000313|EMBL:ELZ21556.1};
OS Haloterrigena salina JCM 13891.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=1227488 {ECO:0000313|EMBL:ELZ21556.1, ECO:0000313|Proteomes:UP000011657};
RN [1] {ECO:0000313|EMBL:ELZ21556.1, ECO:0000313|Proteomes:UP000011657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13891 {ECO:0000313|EMBL:ELZ21556.1,
RC ECO:0000313|Proteomes:UP000011657};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ21556.1}.
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DR EMBL; AOIS01000019; ELZ21556.1; -; Genomic_DNA.
DR RefSeq; WP_008893477.1; NZ_AOIS01000019.1.
DR AlphaFoldDB; M0CE71; -.
DR STRING; 1227488.C477_05741; -.
DR PATRIC; fig|1227488.3.peg.1137; -.
DR eggNOG; arCOG01706; Archaea.
DR eggNOG; arCOG02700; Archaea.
DR OrthoDB; 56234at2157; -.
DR Proteomes; UP000011657; 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 Reference proteome {ECO:0000313|Proteomes:UP000011657}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 140..177
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 78..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 59532 MW; D5591D1788C60F5F CRC64;
MVREFELPDV GEGVAEGELV SWLVEKGDTV SEDQPVAEVE TDKALVEVPA PVNGTVRELH
VDEGEVVPVG TVIISFDVEG EESEATTDEE QERAGEPEGV DTPDGTTDTR AEAEGGESTG
SPEAIGADAE ETATPQDRVF APPRVRRMAR EEGIDLSRLE GSGPGGRITA ADVQAAASGG
PAGGEAQAQL PAETAAESGA TTGDSSGSGG AAVETEGRTE AGSGAEAGTG AASTSESTTP
PTDLESADRE KTLAAPATRR IAREKGIDIN AVPTDEQREG EAFVTPEAVR EYAEAQQRAQ
EADREAVEAG EPVGTKGTDF AEGERERREP FRGVRKRIAE AMVESKYSAP HVTHHDEVDV
TELVEAREEL KPRAEERGIR LTYMPFIMKA VVAALQEFPE MNAVIDEESD EIVYRDYYNV
GVATATDVGL MVPVVENADE KGLLQLSSEM NELVQKARER SISPGELRGS TFTITNVGAI
GGEYATPIIN YPEAGILAIG AIKRKPRVMT DENGTESIEP RSVLTLSLSF DHRLIDGAIA
AQFTNAVMEY LENPSLLLLE
//
