ID F7NRU1_9GAMM Unreviewed; 516 AA.
AC F7NRU1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=Rhein_0474 {ECO:0000313|EMBL:EGM79338.1};
OS Rheinheimera sp. A13L.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM79338.1, ECO:0000313|Proteomes:UP000004282};
RN [1] {ECO:0000313|EMBL:EGM79338.1, ECO:0000313|Proteomes:UP000004282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A13L {ECO:0000313|EMBL:EGM79338.1,
RC ECO:0000313|Proteomes:UP000004282};
RX PubMed=21742876; DOI=10.1128/JB.05636-11;
RA Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.;
RT "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from Pangong
RT Lake, India.";
RL J. Bacteriol. 193:5873-5874(2011).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGM79338.1}.
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DR EMBL; AFHI01000003; EGM79338.1; -; Genomic_DNA.
DR RefSeq; WP_008897371.1; NZ_AFHI01000003.1.
DR AlphaFoldDB; F7NRU1; -.
DR STRING; 506534.Rhein_0474; -.
DR eggNOG; COG0508; Bacteria.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000004282; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
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; 2.
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; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:EGM79338.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:EGM79338.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EGM79338.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 104..179
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 216..253
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 516 AA; 54597 MW; 23DEF504E0C6B5D6 CRC64;
MKKDFILPDI GEGIVECEIV EWLVKEGDRI SEDQPVCDVM TDKALVQIPA VYDGVVTKLY
YAKGDIAKVH APLFEMDTDG VAPAATPASA PAQTPAAVAT GKQLEDFILP DIGEGIVECE
IVEWLIKEGD VLAEDQPVCD VMTDKALVQI PAKYAGKVVK LHYAKGEIAK VHSPLFQQEI
AGTSAPAVVA TPVAAPVCAA KAAASTSAPA GNGKALASPA VRRLARELSI DLSLVPGSGD
KGRVYKDDVK AYANGGATSG VAKAAATPVK AATAATVTTS SGGSRVEPIK GIKAAMARQM
QDSVSTIPHF TYCEEIDLTE LIALRGQLKD QYAKQGIKLT LMPFFMKAMS LAIKQFPIMN
SQVNSDCSEL TYFDDHNIGI AVDSKVGLLV PNIKGCQNKS IVQIAQELTK LTEAAREGRV
SPAELKGGTI TISNIGAIGG TVATPIINKP EVAIVALGKT QLLPRFNAKG EVEGRSLMQI
SWSGDHRVID GGTIARFTNL WKSYLEQPSS MLLSMV
//
