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Database: UniProt
Entry: A0A1I0NFJ7_9EURY
LinkDB: A0A1I0NFJ7_9EURY
Original site: A0A1I0NFJ7_9EURY 
ID   A0A1I0NFJ7_9EURY        Unreviewed;       645 AA.
AC   A0A1I0NFJ7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=dihydrolipoyllysine-residue acetyltransferase {ECO:0000256|ARBA:ARBA00013114};
DE            EC=2.3.1.12 {ECO:0000256|ARBA:ARBA00013114};
GN   ORFNames=SAMN05216285_1650 {ECO:0000313|EMBL:SEV99799.1};
OS   Natrinema salifodinae.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=1202768 {ECO:0000313|EMBL:SEV99799.1, ECO:0000313|Proteomes:UP000183275};
RN   [1] {ECO:0000313|Proteomes:UP000183275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12284 {ECO:0000313|Proteomes:UP000183275};
RA   Varghese N.;
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; FOIS01000002; SEV99799.1; -; Genomic_DNA.
DR   RefSeq; WP_049988652.1; NZ_JROF01000001.1.
DR   AlphaFoldDB; A0A1I0NFJ7; -.
DR   STRING; 1202768.SAMN05216285_1650; -.
DR   eggNOG; arCOG01706; Archaea.
DR   eggNOG; arCOG03686; Archaea.
DR   OrthoDB; 56234at2157; -.
DR   Proteomes; UP000183275; Unassembled WGS sequence.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 2.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR045257; E2/Pdx1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR003718; OsmC/Ohr_fam.
DR   InterPro; IPR036102; OsmC/Ohrsf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 2.
DR   Pfam; PF02566; OsmC; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF82784; OsmC-like; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 2.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 2.
PE   3: Inferred from homology;
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW   Pyruvate {ECO:0000313|EMBL:SEV99799.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183275};
KW   Transferase {ECO:0000313|EMBL:SEV99799.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          141..178
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   DOMAIN          192..229
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          63..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   645 AA;  67719 MW;  6E910D8F633297B2 CRC64;
     MGYIVRMPKL GLEMERGTLL DWAADEGDSV SEGDLIAEVE SEKSVADVEA REDGALRRTY
     LEAGESVPPG TPIGIVAPPE SDISGLESEA TADLEANVEL EDGPKTEIEP AADDQAAEPS
     AAGGADAETT DGDGASADEI KASPRARERA AALGVDLTTV EGTGYQGSIS EADVERAAKE
     ADTGDEDGSE PDASPRARKR AEELGVDLST VEGTGYQGAI SASDVEAAAE SEPAAVDATA
     GGAAPRTLDE ERPFDGMRRT IASRLSESYR EAVHVTVHRE ADAEALFAAA DVASDVLETD
     VSVQDVLLRA VSATLAEHPG FNATFEDDVH KHWSERNLGI AVDVEQGLIA PVLPDVGEKS
     LAEIADERRD LVDRAVSGDY TMDDLQGGTF TVTNLGVLGV ESFDPIINPP QVAILGVDAV
     AERPTRGDDD GVEWRRHLPF DLTFDHRVVD GADAARFLET LVGHVAEPWP LLPDAVAEAA
     DAADGAGGVA AESESEAAEV DGGPAGADAE TEMPGRSVSA ANPEGMRGRI EAGSFEWSYD
     EPESSGGTET GPTPVDVFLG GLASCLSLSA RYQASKRDAA VDEIRVDVDA APEEGSVERI
     EATIQIDSDE DDETLERIVD LAERGCHVSQ LLRADLDLNL TWDQL
//
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