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Database: UniProt
Entry: U1QUV2_9EURY
LinkDB: U1QUV2_9EURY
Original site: U1QUV2_9EURY 
ID   U1QUV2_9EURY            Unreviewed;       322 AA.
AC   U1QUV2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component {ECO:0000313|EMBL:ERH11083.1};
GN   ORFNames=J07HX64_02862 {ECO:0000313|EMBL:ERH11083.1};
OS   halophilic archaeon J07HX64.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales.
OX   NCBI_TaxID=1085028 {ECO:0000313|EMBL:ERH11083.1};
RN   [1] {ECO:0000313|EMBL:ERH11083.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23637883;
RA   Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA   Allen E.E.;
RT   "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL   PLoS ONE 8:E61692-E61692(2013).
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938};
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DR   EMBL; KE356579; ERH11083.1; -; Genomic_DNA.
DR   STRING; 1085028.J07HX64_02862; -.
DR   HOGENOM; CLU_016733_2_1_2; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR023213; CAT-like_dom_sf.
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   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:ERH11083.1};
KW   Pyruvate {ECO:0000313|EMBL:ERH11083.1};
KW   Transferase {ECO:0000313|EMBL:ERH11083.1}.
FT   DOMAIN          94..322
FT                   /note="2-oxoacid dehydrogenase acyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00198"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   322 AA;  34289 MW;  04E1B23A50B58DF5 CRC64;
     MRERPRRSQT VRRPGXXXXX XXTATETAPK ETTAAVTEAT TTTDEPATAV TEAATTPNET
     ATAATETATT AGEPAAVDAV AETGDADTTD TAAVRREPYQ GIRQTIGEAM AESAHTAPHA
     SHHDTAPAGG LVEARQRLKP RAEDEGVHLT YMPFVMKAVA AVLPEYPAMN AQLDEDAGEI
     LYHDRYHIGV AVATDAGLMV PVVEDVDRKG LLELAAEVND LVERARNREL TPDELQGSTF
     TITNFGAIGG EYATPILNYP ETGILGLGEL RQRPVVEDGE VVAGHTLPLS VSIDHRVVDG
     AVSAGFCNDL KTYLEDPIHL LL
//
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