ID A0A023DBT0_9BACI Unreviewed; 435 AA.
AC A0A023DBT0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=pdhC {ECO:0000313|EMBL:GAJ38798.1};
GN ORFNames=GCA01S_008_00430 {ECO:0000313|EMBL:GAJ38798.1};
OS Parageobacillus caldoxylosilyticus NBRC 107762.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX NCBI_TaxID=1220594 {ECO:0000313|EMBL:GAJ38798.1, ECO:0000313|Proteomes:UP000023561};
RN [1] {ECO:0000313|EMBL:GAJ38798.1, ECO:0000313|Proteomes:UP000023561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107762 {ECO:0000313|EMBL:GAJ38798.1,
RC ECO:0000313|Proteomes:UP000023561};
RA Hosoyama A., Hosoyama Y., Katano-Makiyama Y., Tsuchikane K., Ohji S.,
RA Ichikawa N., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Geobacillus caldoxylosilyticus NBRC
RT 107762.";
RL Submitted (APR-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 -!- 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:GAJ38798.1}.
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DR EMBL; BAWO01000008; GAJ38798.1; -; Genomic_DNA.
DR RefSeq; WP_042407307.1; NZ_BAWO01000008.1.
DR AlphaFoldDB; A0A023DBT0; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000023561; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:GAJ38798.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000023561};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 131..168
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 87..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 47458 MW; AF728C7E3F64C9E4 CRC64;
MAFEFKLPDI GEGIHEGEIV KWFVKPGDEV NEDDVLCEVQ NDKAVVEIPS PVKGKVLEIL
VEEGTVATVG QTLITFDAPG YENMTFKGQE QDETKQQEKP QEVSKEEKSE AAAPQTEPAG
QPEVDPNRRV IAMPSVRKYA REKGVDIRLV QGTGKNGRVL KSDIDAFLAG GAAAAQKQEA
PTAKEEKAAA AAAQQPVVLE GEFPETREKM SGIRRAIAKA MVNSKHTAPH VTLMDEVDVT
KLVAHRKKFK EIAAEKGIKL TFLPYVVKAL TSALREFPVL NTSIDDATEE IIHKHYYNIG
IAADTDRGLL VPVIKHADRK PIFALAKEIN ELATKAREGK LMPNEMKGAS CTITNIGSAG
GQWFTPVINH PEVAILGIGR IAEKPIVRDG EIVVAPVLAL SLSFDHRMID GATAQKALNH
IKRLLNDPEL LLMEA
//
