ID C0BKP8_9BACT Unreviewed; 558 AA.
AC C0BKP8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN ORFNames=Flav3CDRAFT_0871 {ECO:0000313|EMBL:EEG43397.1};
OS Flavobacteria bacterium MS024-3C.
OC Bacteria; Bacteroidota; Flavobacteriia.
OX NCBI_TaxID=487797 {ECO:0000313|EMBL:EEG43397.1, ECO:0000313|Proteomes:UP000003631};
RN [1] {ECO:0000313|EMBL:EEG43397.1, ECO:0000313|Proteomes:UP000003631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS024-3C {ECO:0000313|EMBL:EEG43397.1,
RC ECO:0000313|Proteomes:UP000003631};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Woyke T., Xie G., Copeland A., Gonzalez J., Han C., Kiss H., Saw J.,
RA Senin P., Chatterji S., Cheng J.-F., Eisen J.A., Sieracki M.E.,
RA Stepanauskas R.;
RT "Assembling the metagenome, one cell at a time.";
RL Submitted (AUG-2008) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000925,
CC ECO:0000256|RuleBase:RU361137};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU361137};
CC Note=Binds 2 lipoyl cofactors covalently.
CC {ECO:0000256|RuleBase:RU361137};
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:RU361137}.
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:EEG43397.1}.
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DR EMBL; ABVW01000001; EEG43397.1; -; Genomic_DNA.
DR AlphaFoldDB; C0BKP8; -.
DR STRING; 487797.Flav3CDRAFT_0871; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000003631; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
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; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR006257; LAT1.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01349; PDHac_trf_mito; 1.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
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; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:EEG43397.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003631};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361137}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 133..208
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 270..307
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 558 AA; 57797 MW; B2CAC73FD74AF3E4 CRC64;
MAIVVNMPRL SDTMEEGTVA KWLKQVGDVI SEGDILAEIE TDKATMEFES FNEGTLLHIG
IQEGDAAPVD ALLAIIGEKG EDISALLSGG APAAQEASEA SAAEAAEAAV SAAEVTAPVV
VATATATALP EGVIVVNMPR LSDTMEEGTV ATWLKKVGDV IEEGDILAEI ETDKATMEFE
SFNAGTLLHI GIGEGEAAPV DSLLAIIGPK GADISAALNP VAAPVAAKTV ATAPVAVNDA
AAAPVATPTP KAPVADATAV NASVQTGRIF ASPLAKKLAK EKGISLSEVK GTGEQGRIVK
IDIERFTPAA AQSIATTSAT ASAQAPVMAA GEEHYTEVKN SQMRKVIAKR LGESKFSAPH
YYLTVEVAMD NAMASRAQIN SLPDTKVSFN DMVLKASAMA LKKHPQVNTT WQGDTTRFNS
HVHMGVAVSV PDGLVVPVVR FADQQSLSQI GAAVKDLAGK ARDKKLTPAE MEGSTFTVSN
LGMFGIQEFT SIINQPNSAI LSVGAIVQKP VVKEGAIVVG NTMKITLACD HRTVDGATAA
AFLQTLQAFL ENPVTMLA
//