ID A0A345GUK0_9FLAO Unreviewed; 553 AA.
AC A0A345GUK0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN Name=pdhC {ECO:0000313|EMBL:AXG67988.1};
GN ORFNames=KORDIASMS9_00170 {ECO:0000313|EMBL:AXG67988.1};
OS Kordia sp. SMS9.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=2282170 {ECO:0000313|EMBL:AXG67988.1, ECO:0000313|Proteomes:UP000253780};
RN [1] {ECO:0000313|EMBL:AXG67988.1, ECO:0000313|Proteomes:UP000253780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS9 {ECO:0000313|EMBL:AXG67988.1,
RC ECO:0000313|Proteomes:UP000253780};
RA Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Clarke A.K.,
RA Godhe A.;
RT "Genome Sequence of Kordia sp. Strain SMS9 Isolated from a Culture of the
RT Diatom Skeletonema marinoi.";
RL Submitted (JUL-2018) 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:ARBA00043782,
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}.
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DR EMBL; CP031153; AXG67988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345GUK0; -.
DR KEGG; kos:KORDIASMS9_00170; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000253780; Chromosome.
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|RuleBase:RU361137,
KW ECO:0000313|EMBL:AXG67988.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:AXG67988.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253780};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:AXG67988.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 125..200
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 256..293
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 85..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 58612 MW; 6A496658842E2AFD CRC64;
MAEIINMPRL SDTMEEGVVA SWLKQVGDTV EEGDILAEIE TDKATMEFES FHEGTLLYIG
VQEGETAPVD TLLAIIGEEG EDVDALVKGG GTSETKEEPK GETTETKTEE APKSTTEKVE
MPAGAIVVTM PRLSDTMEEG TVASWLKQVG DTIEEGDILA EIETDKATME FESFNEGTLL
YIGVKEGETA PVDSILAIIG EKGTDVDTVL KAAASGDSAT SSSEETVSKP SGNLAAESKA
EAPKASGSES SGGRIIASPL AKKIAADKGI DLTQVKGSGD HGRIIKRDVE NFTPAAVAAP
VAKATPSVAT PAAESVPAIT PFVPAGEESS EEVKNSQMRK TIARRLGESK FSAPHYYLTV
ELDMDNAIAS RKTINAIPDI KVSFNDMIVK ACAMALRKHP QVNTTWNDNS TTYHKHIHVG
VAVAVDEGLL VPVLKFADQM SLTTIGGKVR ELAGKARNKK ISPAEMDGST FTISNLGMFG
ILEFTSIINQ PNSAILSVGT IVQKPVVKNG EIVVGNTMKV TLACDHRTVD GATGAQFLQT
VKQYVENPVT MLA
//
