ID A0A127FB52_STEDE Unreviewed; 478 AA.
AC A0A127FB52;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ACG33_11190 {ECO:0000313|EMBL:AMN47654.1};
OS Steroidobacter denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Steroidobacterales;
OC Steroidobacteraceae; Steroidobacter.
OX NCBI_TaxID=465721 {ECO:0000313|EMBL:AMN47654.1, ECO:0000313|Proteomes:UP000070250};
RN [1] {ECO:0000313|EMBL:AMN47654.1, ECO:0000313|Proteomes:UP000070250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18526 {ECO:0000313|EMBL:AMN47654.1,
RC ECO:0000313|Proteomes:UP000070250};
RA Yang F.-C., Chen Y.-L., Yu C.-P., Tang S.-L., Wang P.-H., Ismail W.,
RA Wang C.-H., Yang C.-Y., Chiang Y.-R.;
RT "A Comprehensive Approach to Explore the Metabolic and Phylogenetic
RT Diversity of Bacterial Steroid Degradation in the Environment: Testosterone
RT as an Example.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
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; CP011971; AMN47654.1; -; Genomic_DNA.
DR RefSeq; WP_066923288.1; NZ_CP011971.1.
DR AlphaFoldDB; A0A127FB52; -.
DR STRING; 465721.ACG33_11190; -.
DR KEGG; sdf:ACG33_11190; -.
DR PATRIC; fig|465721.4.peg.2388; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000070250; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; 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:SF2; DIHYDROLIPOYLLYSINE-RESIDUE 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:AMN47654.1}; Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:AMN47654.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070250};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AMN47654.1}.
FT DOMAIN 2..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 180..217
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 88..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 49827 MW; 3B335EAD9B5AAFAD CRC64;
MAQDITVPDL GDFKDVEVID VLITPGDVIE VDTPLITIET EKATMDVPST VAGTITAVAL
KKGDRVSKGS LIAQFEAGVP AASTERIQEA SQTVSQTVSQ AASPAAAQPA SAESPSALQP
PAAVFGDAGA PTATSPAAAS RSPVGADVVP DDKDGKGEAP VSLTAASSFV MGEAGFARAY
ASPSVRRFAR ELGVDLTQIE GSGLKGRITP DDVKAWVKRT LASGVSSAGG GALPKIPEID
FAKFGPIESQ PLGRIQKISG PHLQASWLNI PHVWQMDEAD ITAMDAARIE SRQKALDAGI
KLTPLAFILR ACVQALQEFP FVNSSLDASG ANLVLKKYMH LGFAADTPQG LLVPVIRDAD
KKDIYELARE LGTLSQKARE GKLSAADMQG ASFTVSSLGG IGGTSFTPII NAPEVAILGV
ARASMKPVWQ EGQFVPRLIL PFTLAYDHRV IDGAAGARFT SFLARKLADV NGLLEAVP
//
