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Database: UniProt
Entry: F0RTH1_SPHGB
LinkDB: F0RTH1_SPHGB
Original site: F0RTH1_SPHGB 
ID   F0RTH1_SPHGB            Unreviewed;       437 AA.
AC   F0RTH1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
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=SpiBuddy_2226 {ECO:0000313|EMBL:ADY14045.1};
OS   Sphaerochaeta globosa (strain ATCC BAA-1886 / DSM 22777 / Buddy)
OS   (Spirochaeta sp. (strain Buddy)).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Sphaerochaetaceae;
OC   Sphaerochaeta.
OX   NCBI_TaxID=158189 {ECO:0000313|EMBL:ADY14045.1, ECO:0000313|Proteomes:UP000008466};
RN   [1] {ECO:0000313|Proteomes:UP000008466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1886 / DSM 22777 / Buddy
RC   {ECO:0000313|Proteomes:UP000008466};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Mikhailova N., Pagani I., Ritalahti K.M., Loeffler F.E.,
RA   Woyke T.;
RT   "Complete sequence of Spirochaeta sp. Buddy.";
RL   Submitted (FEB-2011) 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; CP002541; ADY14045.1; -; Genomic_DNA.
DR   RefSeq; WP_013607894.1; NC_015152.1.
DR   AlphaFoldDB; F0RTH1; -.
DR   STRING; 158189.SpiBuddy_2226; -.
DR   KEGG; sbu:SpiBuddy_2226; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_2_12; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000008466; Chromosome.
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:ADY14045.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008466};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ADY14045.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          118..155
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   437 AA;  45886 MW;  844017A26E8633DC CRC64;
     MAQQVVMPKQ GNSVESCIIV EWNVQLGDKV AIGDVLCSAE TDKSTIDVES TAEGVVLARL
     FEEGADVPVM VPIAVIGEAG EKVETAAQEE AKQQAETVNH VASSEVEKPL VTAAQAIGAS
     PRARQLASSL GISLENVQPT GPKGRIIERD VEAAKGQPLS PVAREQALEQ GLKAPLSGSG
     IGGRVLASDL VAKPVEAAAV AVPSLEDVTE IAVKGVRKVT ARRMMESIHS TCQLSLHAFA
     DARALKRLRA GFKASKPELG LQAITINDLV LFAVSRTLTQ FPAFNAHFLG DKILRFSHVH
     LGVATDTAKG LLVPVLRNSE LLSLKQLSEG TKALVGKCKA GTAQPDELSG STFTVSNVGS
     FGIEAFTPVL NVPEVAILGV GTITLKPIED EDGDVVFIEH IGLSLTMDHQ AVDGADAARF
     LKALMDNIAS IDLLLAL
//
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