ID W2URN0_9FLAO Unreviewed; 542 AA.
AC W2URN0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=P278_00350 {ECO:0000313|EMBL:ETN96609.1};
OS Zhouia amylolytica AD3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zhouia.
OX NCBI_TaxID=1286632 {ECO:0000313|EMBL:ETN96609.1, ECO:0000313|Proteomes:UP000018850};
RN [1] {ECO:0000313|Proteomes:UP000018850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD3 {ECO:0000313|Proteomes:UP000018850};
RA Jin H., Jeon C.O.;
RT "Draft genome sequence from a member of Zhouia, isolated tidal flat.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN96609.1, ECO:0000313|Proteomes:UP000018850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD3 {ECO:0000313|EMBL:ETN96609.1,
RC ECO:0000313|Proteomes:UP000018850};
RX PubMed=27151796;
RA Jia B., Jin H.M., Lee H.J., Jeon C.O.;
RT "Draft Genome Sequence of Zhouia amylolytica AD3, Isolated from Tidal Flat
RT Sediment.";
RL Genome Announc. 4:0-0(2016).
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}.
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:ETN96609.1}.
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DR EMBL; AYXY01000001; ETN96609.1; -; Genomic_DNA.
DR RefSeq; WP_038260547.1; NZ_AYXY01000001.1.
DR AlphaFoldDB; W2URN0; -.
DR STRING; 376730.SAMN04487906_3341; -.
DR PATRIC; fig|1286632.3.peg.35; -.
DR eggNOG; COG0508; Bacteria.
DR Proteomes; UP000018850; 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|RuleBase:RU361137,
KW ECO:0000313|EMBL:ETN96609.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:ETN96609.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018850};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:ETN96609.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 121..196
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 94..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 57839 MW; 3FB818707522D45E CRC64;
MAEIINMPRL SDTMEEGTVA KWLKKVGDKV EEGDILAEIE TDKATMEFES FYSGTLLHIG
VAEGETTKVD ELLAVIGDEG EDVNAIINGA QATETVEEKT ETPQETTADK AAPAAEMPEG
VEVVTMPRLS DTMEEGTVAS WLKKIGDEVT EGDILAEIET DKATMEFESF YAGTLLYIGV
QEGESAPVDS ILAVIGPKGT DVDAVLNASK SGGSAQTETP KSEPKKDTAV AKPEPVVESK
PAATVTTSTT AGGRILASPL AKKMASEKGI DLANVQGTGE NGRIVKKDIE SYKPVETSAP
ASTEVSGVQP FVPSGQESVE EVKNSQMRKT IAKRLAESKF NAPHYYLTIE VDMDNAMASR
KQINNLPDTK VSFNDMVVKA CAMALKKHPQ VNTSWKGDTT QYNHHVHVGV AVAVDEGLVV
PVLKFTDQLG LTQIGSQVKD LAGKARNKKL TPAEMEGSTF TVSNLGMFGI QEFTSIINQP
NSAILSVGAI VQKPVVKDGQ IVVGNTMKVT LACDHRTVDG ATGAQFLQTL KAYMENPVTM
LA
//
