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Database: UniProt
Entry: L0I9C5_HALRX
LinkDB: L0I9C5_HALRX
Original site: L0I9C5_HALRX 
ID   L0I9C5_HALRX            Unreviewed;       520 AA.
AC   L0I9C5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase component {ECO:0000313|EMBL:AGB14821.1};
GN   OrderedLocusNames=Halru_0169 {ECO:0000313|EMBL:AGB14821.1};
OS   Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halovivax.
OX   NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB14821.1, ECO:0000313|Proteomes:UP000010846};
RN   [1] {ECO:0000313|Proteomes:UP000010846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18193 / JCM 13892 / XH-70
RC   {ECO:0000313|Proteomes:UP000010846};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Halovivax ruber XH-70.";
RL   Submitted (SEP-2011) 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; CP003050; AGB14821.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0I9C5; -.
DR   STRING; 797302.Halru_0169; -.
DR   KEGG; hru:Halru_0169; -.
DR   eggNOG; arCOG01706; Archaea.
DR   eggNOG; arCOG02700; Archaea.
DR   HOGENOM; CLU_016733_10_0_2; -.
DR   OrthoDB; 56234at2157; -.
DR   Proteomes; UP000010846; Chromosome.
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:AGB14821.1};
KW   Pyruvate {ECO:0000313|EMBL:AGB14821.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010846};
KW   Transferase {ECO:0000313|EMBL:AGB14821.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          135..172
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          83..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  55598 MW;  A2AA696D8D5238AD CRC64;
     MTMEFTLPDV GEGVAEGELV SWLVEPGDTV SEDQPVAEVE TDKALVEVPS PTNGTVRELH
     WAEGDVVPVG DLFITYNVEG EDDQDVTEQG ADTASAEQGG ADAADDADAT PSTESEAGGE
     ADESGETDTP SGRVFAPPSV RRLARELGVD IETVEGTGPS GRLTEGDVRA AAESDESAPA
     GTGDEQPTET GADASTAPES TQSAATRGGA TAQVESADRE RTLAAPATRK LAEEEGVDLN
     TVPTDEERDG EAFVTPEAVT EYAQAQRQAQ EADAAAVATG ETGPRERREP FKGVRKTIAD
     AMVESKFSAP HVTHHDEVDV TKLVETRERL KPIAEEQGIR LTFMPFIMKA VVAALEEYPE
     MNAVIDEDNE EVVYRNYHNI GVAAATDVGL MVPVVDDADH KGMLQLSSEM NELVQKARER
     TISPDELQGS TFTITNIGGI GGEYATPILN YPESGILAVG EIKRKPRVVT DENGEESIEP
     RSVMTLSLSF DHRLIDGAVG AQFTNEVMKY LEEPERLLLE
//
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