ID F8A7P7_CELGA Unreviewed; 488 AA.
AC F8A7P7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=Celgi_3089 {ECO:0000313|EMBL:AEI13580.1};
OS Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio gilvus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI13580.1, ECO:0000313|Proteomes:UP000000485};
RN [1] {ECO:0000313|Proteomes:UP000000485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL Submitted (APR-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; CP002665; AEI13580.1; -; Genomic_DNA.
DR RefSeq; WP_013885097.1; NC_015671.1.
DR AlphaFoldDB; F8A7P7; -.
DR STRING; 593907.Celgi_3089; -.
DR KEGG; cga:Celgi_3089; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_11; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000000485; 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; 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|RuleBase:RU003423,
KW ECO:0000313|EMBL:AEI13580.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000000485};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AEI13580.1}.
FT DOMAIN 4..79
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 191..228
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 488 AA; 50403 MW; D19400A77568CC58 CRC64;
MPTYQQFPLP DAGEGLTEAE IVEWHVAVGD TVEVNQTIVE IETAKSLVDL PCPWAGVVTR
ILVETGTTVD VGTPIIEIDT DPTGAAPAAP EVAGQGAGPV HHVGGAERHR GVEPGGSDEI
EAARAAAADV TPAREAVLVG YGLADAGATR RPRGAQGDAP AAVASAPAAA PAVPAAAAPA
PTTPARAGRV LAKPPVRKLA RDLGVDLDSV SPTGPGGIVT REDVLGRAAQ AEARTLATYP
GDDMPWLASG TVSADGRATR VPVKSVRKRT AEAMVASAFT APHVTVFHTV DVTRTMKLVE
KLRADRDFAD VRVTPLLIAA KALLLAVRRH PEINASWDEA AQEIVYKHYV NLGIAAATPR
GLVVPNVKDA HRLGLLELAT ALGELTATAR AGRTSPADMA DGTITVTNVG VFGIDTGTPI
LNPGEAAILA FGAIRLQPWV HKGKVKVRHV TQLALSFDHR LVDGGLGSRV LADVAAVLAD
PAQALVWG
//
