ID   C5D8I2_GEOSW            Unreviewed;       398 AA.
AC   C5D8I2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=GWCH70_3162 {ECO:0000313|EMBL:ACS25820.1};
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS25820.1};
RN   [1] {ECO:0000313|EMBL:ACS25820.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70 {ECO:0000313|EMBL:ACS25820.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) 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}.
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DR   EMBL; CP001638; ACS25820.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5D8I2; -.
DR   STRING; 471223.GWCH70_3162; -.
DR   KEGG; gwc:GWCH70_3162; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_9; -.
DR   OrthoDB; 9805770at2; -.
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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          101..138
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   COILED          284..311
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   398 AA;  43952 MW;  3D6EA08F70F2BB40 CRC64;
     MRYEFKLPDI GEGLHEAEIV RWFIQEGDEV SVDQPIAEIQ TDKAMVEMTT PVAGKVVALA
     GPEGATVKVG EPLIIVDQQK ASDHEEAAAE SKPAQRKKRV IAAPSVRKRA REMGVPIEEV
     EGTGEGGRVT LADLERYVKE RESASAAVAP ALEATEMPTV HKQTVNEERI PIRGLRKKIA
     EKMVKSAYTA PHVTGMDEID VTKLVEIRTG LVKQLETESV KLTYLPFVIK AVTRALKEHP
     IFNATIDEET NEIVLKKEYH IGIATATKEG LVVPVIKHAD QKSIRELAIE LAELSEKAHR
     HTLRVDELQG STFTITSTGA NGGWFATPII NYPEVAILGV HSIKRKPAVI GDEIVIRDMM
     GMSLTFDHRV IDGEPAGRFM RTVAQILEHP EQLLLDVR
//