ID A0A0G9MQR6_9SPHN Unreviewed; 437 AA.
AC A0A0G9MQR6;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=AAW01_02595 {ECO:0000313|EMBL:KLE32924.1}, BMF35_a1940
GN {ECO:0000313|EMBL:APE28769.1};
OS Aurantiacibacter gangjinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=502682 {ECO:0000313|EMBL:KLE32924.1, ECO:0000313|Proteomes:UP000053070};
RN [1] {ECO:0000313|EMBL:KLE32924.1, ECO:0000313|Proteomes:UP000053070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K7-2 {ECO:0000313|EMBL:KLE32924.1,
RC ECO:0000313|Proteomes:UP000053070};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacr gangjinensis K7-2.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:APE28769.1, ECO:0000313|Proteomes:UP000183202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC1.15024 {ECO:0000313|EMBL:APE28769.1,
RC ECO:0000313|Proteomes:UP000183202};
RA Xu L., Wu Y.-H., Cheng H., Zhou Y.-G., Wu M., Cheng L., Xu X.-W.;
RT "Complete genome sequence of two-chromosomal Erythrobacter gangjinensis
RT CGMCC 1.15024T, isolated from seawater.";
RL Submitted (NOV-2016) 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 1 lipoyl cofactor 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; CP018097; APE28769.1; -; Genomic_DNA.
DR EMBL; LBHC01000001; KLE32924.1; -; Genomic_DNA.
DR RefSeq; WP_047005774.1; NZ_LBHC01000001.1.
DR AlphaFoldDB; A0A0G9MQR6; -.
DR STRING; 502682.BMF35_a1940; -.
DR KEGG; egn:BMF35_a1940; -.
DR PATRIC; fig|502682.8.peg.529; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000053070; Unassembled WGS sequence.
DR Proteomes; UP000183202; Chromosome i.
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; 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; 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; 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; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361137,
KW ECO:0000313|EMBL:APE28769.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:APE28769.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053070};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:APE28769.1}.
FT DOMAIN 2..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 140..177
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 83..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 45131 MW; 2AD044F65F58EDEA CRC64;
MPIAIKMPAL SPTMEEGTLA KWLVKVGDQV SAGDIMAEIE TDKATMEFEA VDEGVIAHIQ
VDEGTEGVAV GTVIATLAEE GEDAGDVQPM GDGAAAPAAA ATPAPVEDAP APKEAATPAP
SPSPTPAPTP AAAPSGDRII ASPLARRIAE QKGIDLTGVK GSGPNGRIVK ADVENAQPGT
AKADKEAAAP ATPTDALPVA KPEAADFGIP HEVEKLSSMR KTIARRLTES KQQVPHIYLT
VDIRLDALLK LRSELNAALE PQGVKLSVND LMIKALGKSL EAVPACNVQF AGDTMLKFTR
ADVSVAVSIP NGLITPIVTD AGAKSVSKIS TEMKDLATRA KDGKLAPEEY QGGTASLSNM
GMFGIKQFEA VINPPQGMIM AIGAGDKRPY VVDDSLQIAS VMSATGSFDH RAIDGADGAQ
LMKAFKEMIE APLGLVA
//
