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Database: UniProt/TrEMBL
Entry: D5BZS8_NITHN
LinkDB: D5BZS8_NITHN
Original site: D5BZS8_NITHN 
ID   D5BZS8_NITHN            Unreviewed;       374 AA.
AC   D5BZS8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=Nhal_1211 {ECO:0000313|EMBL:ADE14373.1};
OS   Nitrosococcus halophilus (strain Nc4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE14373.1, ECO:0000313|Proteomes:UP000001844};
RN   [1] {ECO:0000313|Proteomes:UP000001844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG   US DOE Joint Genome Institute;
RA   Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA   Klotz M.G.;
RT   "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT   aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000256|ARBA:ARBA00011484}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; CP001798; ADE14373.1; -; Genomic_DNA.
DR   RefSeq; WP_013032264.1; NC_013960.1.
DR   AlphaFoldDB; D5BZS8; -.
DR   STRING; 472759.Nhal_1211; -.
DR   KEGG; nhl:Nhal_1211; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_6; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000001844; 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; 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:SF12; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 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:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:ADE14373.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001844};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ADE14373.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          120..157
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   374 AA;  40594 MW;  8ED7BBCF207BDB30 CRC64;
     MNRIFKLPDL GEGLTDAEIV EWHVKVGDEV KMDQPLVAVE TAKAIVDIPS PYQGRIDKLY
     GESGDIIHVD DPLVEFETEG AQPQPEKRED TGTVVGKVET GKEVVQETAT RVGQVPSGIK
     ATPAVRALAH RLDVDLSIVT PTGADGMVTA TDVQRVAKIL AEVGPLEPLR GVRRTMARAM
     ATAHAEVVPV TVNDDADIQA WSPEEDITLR LIRAIVTACQ AEPALNAWYD SHAIGRRILK
     KIDLGIAVDT PDGLFVPVLR DVGNREPANL RQGLDAIKQA VRERKLPPEE LRGYTFTLSN
     FGTFGGRYAD PVVIPPTVAI LGAGRLHEAV VPVNGKPEIH RILPLSLTFD HRSVTGGEAT
     RFLMVAIQDL EKAE
//
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