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Database: UniProt
Entry: C0BKP8_9BACT
LinkDB: C0BKP8_9BACT
Original site: C0BKP8_9BACT 
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
//
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