ID D4GSS6_HALVD Unreviewed; 495 AA.
AC D4GSS6; L9UNM0;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Dihydrolipoamide S-acyltransferase {ECO:0000313|EMBL:ADE04485.1};
DE EC=2.3.1.- {ECO:0000313|EMBL:ADE04485.1};
GN Name=dsa2 {ECO:0000313|EMBL:ADE04485.1};
GN OrderedLocusNames=HVO_0666 {ECO:0000313|EMBL:ADE04485.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE04485.1, ECO:0000313|Proteomes:UP000008243};
RN [1] {ECO:0000313|EMBL:ADE04485.1, ECO:0000313|Proteomes:UP000008243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
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; CP001956; ADE04485.1; -; Genomic_DNA.
DR RefSeq; WP_004044269.1; NZ_AOHU01000097.1.
DR AlphaFoldDB; D4GSS6; -.
DR STRING; 309800.HVO_0666; -.
DR PaxDb; 309800-C498_15393; -.
DR EnsemblBacteria; ADE04485; ADE04485; HVO_0666.
DR GeneID; 8926723; -.
DR KEGG; hvo:HVO_0666; -.
DR PATRIC; fig|309800.29.peg.2976; -.
DR eggNOG; arCOG01706; Archaea.
DR HOGENOM; CLU_016733_10_2_2; -.
DR OrthoDB; 56234at2157; -.
DR Proteomes; UP000008243; 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; 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; 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; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 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 Acyltransferase {ECO:0000313|EMBL:ADE04485.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Reference proteome {ECO:0000313|Proteomes:UP000008243};
KW Transferase {ECO:0000313|EMBL:ADE04485.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 149..186
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT DOMAIN 199..236
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 86..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 50719 MW; 11A6D79C7BE7D4CD CRC64;
MAYVVKMPKL GLEMKSGELS AWLVSEGDEV TEGDPIAEIE SEKTTAEIDA KEDGVLRRVV
LAEGESTAPG GALAIVAGAD EDISGLEADA GVGEGGSEPV ATDDSAGDSS PTEVTETTET
AATGGGDASS VAQSRSRGSD GASENGEVRA SPRAKRLADD LGVDLTTVEG TGPQGAITES
DVETAAESAT ATAAEKRVFA PPSARRLARE LGVDIEAVEG TGQNGRITES DVRAAGGATA
AATDSSAAGA ATTAATDATA ASEPAETERP LSGMRRTIAD RLGESYREAV HVTVDRRADA
EELLAAANAA ADALGVDVSI TDVLLLALSA SLDEHPEFNA TFEDGVHRLH GEHNVCIAVD
VDEGLIAPVV RDVASLSLSE LAETRAETTQ RALSGDFTMD DLSGGTFTVS NLGVLGVESF
DPIINPPQVA ILGVNTIRRE AVPTDDGDVA VRRVISFSLS FDHRIVDGAD AARMLGTLVE
HVENPWPLVI AAGGR
//
