ID Q5UYG4_HALMA Unreviewed; 545 AA.
AC Q5UYG4;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE SubName: Full=2-oxo acid dehydrogenase subunit E2 {ECO:0000313|EMBL:QCP92374.1};
DE SubName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000313|EMBL:AAV47689.1};
DE EC=2.3.1.12 {ECO:0000313|EMBL:AAV47689.1};
GN Name=pdhC2 {ECO:0000313|EMBL:AAV47689.1};
GN OrderedLocusNames=rrnAC2955 {ECO:0000313|EMBL:AAV47689.1};
GN ORFNames=E6P14_16465 {ECO:0000313|EMBL:QCP92374.1};
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569 {ECO:0000313|EMBL:AAV47689.1, ECO:0000313|Proteomes:UP000001169};
RN [1] {ECO:0000313|EMBL:AAV47689.1, ECO:0000313|Proteomes:UP000001169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:AAV47689.1}, and ATCC 43049 / DSM
RC 3752 / JCM 8966 / VKM B-1809 {ECO:0000313|Proteomes:UP000001169};
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2] {ECO:0000313|EMBL:QCP92374.1, ECO:0000313|Proteomes:UP000298722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:QCP92374.1,
RC ECO:0000313|Proteomes:UP000298722};
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) 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; AY596297; AAV47689.1; -; Genomic_DNA.
DR EMBL; CP039138; QCP92374.1; -; Genomic_DNA.
DR RefSeq; WP_011224531.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5UYG4; -.
DR STRING; 272569.rrnAC2955; -.
DR PaxDb; 272569-rrnAC2955; -.
DR EnsemblBacteria; AAV47689; AAV47689; rrnAC2955.
DR GeneID; 40153783; -.
DR KEGG; hma:rrnAC2955; -.
DR PATRIC; fig|272569.17.peg.3514; -.
DR eggNOG; arCOG01706; Archaea.
DR HOGENOM; CLU_016733_10_0_2; -.
DR OMA; HPCIMAP; -.
DR Proteomes; UP000001169; Chromosome I.
DR Proteomes; UP000298722; Chromosome.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
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; 1.
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; 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; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:AAV47689.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Pyruvate {ECO:0000313|EMBL:AAV47689.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001169};
KW Transferase {ECO:0000313|EMBL:AAV47689.1}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 130..167
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 81..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..100
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 56241 MW; 4D3834264F906BC8 CRC64;
MFEFNLPDLG EGVAEGEVLT WRVSPGDAVT EDQVLAEVET DKAAVDVPSP VDGVVQELHA
EVGEMVQTGE VLITIAEEGD AETADAAASD TDEAESAGAD TEEADSAASE AAAADEQSGA
STSTADGRVF ASPSVRRLAR EKGVDIAAVD GSGPGGRVTE GDVEAATASA DEATASDDSP
TSVVSKASDD GDSPTAAVSQ VDAGDTDDGT AVKSAVKSVS GDGQEAASRD QTLATPATRK
AARELDVNID AVPTDQTRDG QPYVDEAAVR TYAEAQQAAQ AADAEAVSAE GGAAGTAAEA
GGAGAETTAV ETGDGERREP YRGVRRSIGE QMARSRREVP HATHHDQVVV SGLVEARERL
APLAEERDVT LTYTPFVVKC VAAALDKHPV LNTALDTENE EIVYRDAHNI GVAAATDHGL
VVPVVNDVDG KGLVELAGEV NDLVGRARER DIERSEMQGG TFTVTNFGVI GGEYASPIIN
VPETAILGIG ALKERPVAED GEVVAKPTLP LSLAIDHRVI DGADAARFVN TLKEYLSDPT
RLLLE
//