ID K2JHI5_9RHOB Unreviewed; 395 AA.
AC K2JHI5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=B30_02775 {ECO:0000313|EMBL:EKE74613.1};
OS Celeribacter baekdonensis B30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE74613.1, ECO:0000313|Proteomes:UP000006762};
RN [1] {ECO:0000313|EMBL:EKE74613.1, ECO:0000313|Proteomes:UP000006762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B30 {ECO:0000313|EMBL:EKE74613.1,
RC ECO:0000313|Proteomes:UP000006762};
RA Wang W.;
RT "Celeribacter baekdonensis B30 Genome Sequencing.";
RL Submitted (SEP-2012) 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}.
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:EKE74613.1}.
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DR EMBL; AMRK01000001; EKE74613.1; -; Genomic_DNA.
DR RefSeq; WP_009570480.1; NZ_AMRK01000001.1.
DR AlphaFoldDB; K2JHI5; -.
DR STRING; 1208323.B30_02775; -.
DR PATRIC; fig|1208323.3.peg.570; -.
DR eggNOG; COG0508; Bacteria.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000006762; 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; 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:SF1; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT 3 OF PYRUVATE 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:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000006762};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 127..164
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 79..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 40770 MW; 9887F9F7D41788D4 CRC64;
MGIFTMPSLG ADMEAGTLVE WLVKPGDEVH RGDVLAVVET QKGAIEIECF GDGRVLELQA
DLGATLPVGA PLALILGPGE VAPEPKEPEA PAADTKPEAV PAQALADTPE VAPDPAVATP
LPHGATAASP AARARASELG IDLATVTGSG PAGAVLLKDL EVRKPSAAIV QTASPMLEMR
KAIAAAMARS KQTIPHFYLS ETIDVQPALE WVEARNADRP PSDRLLLGAL FVRATALAAA
KVPSVNGQFV DGALRPTDRV NIGVAVALRG GGLVAPALID AGAMSVDETM SGMRDLVFRA
RAGRLRSSEV TEGTITISSL GAVGAEAMAG VIFPPQVALV GLGAPKLRPW IVEGAVEPRT
VVTLTLSVDH RVSDGRQAAR FIAEFQSHIA SPETL
//
