ID A0A095C5U5_9SPHN Unreviewed; 433 AA.
AC A0A095C5U5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=FG95_00612 {ECO:0000313|EMBL:KGB58756.1};
OS Sphingopyxis sp. LC363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB58756.1, ECO:0000313|Proteomes:UP000029625};
RN [1] {ECO:0000313|EMBL:KGB58756.1, ECO:0000313|Proteomes:UP000029625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC363 {ECO:0000313|EMBL:KGB58756.1,
RC ECO:0000313|Proteomes:UP000029625};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (MAY-2014) 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:KGB58756.1}.
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DR EMBL; JNFC01000005; KGB58756.1; -; Genomic_DNA.
DR RefSeq; WP_037553902.1; NZ_JNFC01000005.1.
DR AlphaFoldDB; A0A095C5U5; -.
DR STRING; 1120705.FG95_00612; -.
DR PATRIC; fig|1120705.3.peg.613; -.
DR eggNOG; COG0508; Bacteria.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000029625; 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: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:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:KGB58756.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000029625};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:KGB58756.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 151..186
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 122..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 46193 MW; 45B1D0BC3C43D6EE CRC64;
MARYSFRLPD IGEGIAEAEI VAWHVRVGER VEEDAQLADM MTDKATVEME SPVSGIVVEL
AGEVGDLIPI GSTLAVIETD GDGEGEVEAP PADTPIEEEI VSETPGAEEV SDAEAVSLPV
AEGPVEPTPA VSETTPPPTP PASGRGDKAV LASPAVRARA KDLGIDLSQV QSDGDRVRHA
DLDAFLRYSA GQGYHAPGAS RARADEPIKV IGMRRKIAEN MAASKRAIPH FTYVEEMDVT
ALEEMRADLN ANRGGRPKLT MLPFLIVAIC RTIPEFPMIN ARYDDEGGVV TRHGAVHLGM
ATQTDAGLMV PVIRDAQDKN VWQLASEIAR LAEAARTGKA KVEELTGGTL TVTSLGPLGG
IATTPVINRP EVAIIGPNKI VERPVFDGDD IRRAKLMNLS ISCDHRVVDG WDAASYVQAL
KKLIETPVLL FAD
//
