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Database: UniProt
Entry: J2ZH63_9EURY
LinkDB: J2ZH63_9EURY
Original site: J2ZH63_9EURY 
ID   J2ZH63_9EURY            Unreviewed;       526 AA.
AC   J2ZH63;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase component {ECO:0000313|EMBL:EJN60040.1};
GN   ORFNames=HSB1_21980 {ECO:0000313|EMBL:EJN60040.1};
OS   Halogranum salarium B-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae.
OX   NCBI_TaxID=1210908 {ECO:0000313|EMBL:EJN60040.1, ECO:0000313|Proteomes:UP000007813};
RN   [1] {ECO:0000313|EMBL:EJN60040.1, ECO:0000313|Proteomes:UP000007813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-1 {ECO:0000313|EMBL:EJN60040.1,
RC   ECO:0000313|Proteomes:UP000007813};
RX   PubMed=23144405; DOI=10.1128/JB.01815-12;
RA   Kim K.K., Lee K.C., Lee J.S.;
RT   "Draft Genome Sequence of the Extremely Halophilic Archaeon Halogranum
RT   salarium B-1T.";
RL   J. Bacteriol. 194:6659-6659(2012).
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:EJN60040.1}.
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DR   EMBL; ALJD01000004; EJN60040.1; -; Genomic_DNA.
DR   RefSeq; WP_009367280.1; NZ_ALJD01000004.1.
DR   AlphaFoldDB; J2ZH63; -.
DR   PATRIC; fig|1210908.3.peg.2104; -.
DR   eggNOG; arCOG01706; Archaea.
DR   OrthoDB; 56234at2157; -.
DR   Proteomes; UP000007813; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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   Acyltransferase {ECO:0000313|EMBL:EJN60040.1};
KW   Pyruvate {ECO:0000313|EMBL:EJN60040.1};
KW   Transferase {ECO:0000313|EMBL:EJN60040.1}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          127..164
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          81..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..111
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  55614 MW;  A06347B322FF4ACF CRC64;
     MGSKDFKLPD VGEGVAEGEL VSWLVGPGDT VEEDQPVAEV ETDKALVEVP SPYNGTVKEL
     HVEEGTMVPV GDVIITYEVE GEGDESAEAE PEPEAEETAE AEAEASAEAE TAESEQAETS
     AKGGRVFAAP SARRLARELG VDIAAVSGSG PSGRVTDADV RQAAESEAGA SASAETESEA
     QEGGGPRDVD VGGKSSVTKR GEAGNGQQPS DVEAAGRDRT LAAPATRRTA KEQGVDLNDV
     PATEMRDGEA FVSAAAVTEY AEAQQAAQEA DAQAVAEAGA VADEETASAT SEGGISGERI
     PYRGVRRTIG EAMQNSKFTA PHVTHHDSTD VSALVELRAE LKEVAAERDV RLSYMPFVMK
     AIAAALKQYP YMNATLDEEN EEIVLRDEYH IGVATATDAG LMVPVVENVD QKGLLQIAEE
     MNDKIERARD RSIGRDELRG STFTITNFGV VGGEYATPII NYPEVGIMGL GELKERAVVE
     DGDVVARHTL PLSLSIDHRI LDGAVAAQFA NKVMEYLQHP KLLLLE
//
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