ID A0A0H4VG43_9SPHN Unreviewed; 431 AA.
AC A0A0H4VG43;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=CP97_10070 {ECO:0000313|EMBL:AKQ43365.1};
OS Aurantiacibacter atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1648404 {ECO:0000313|EMBL:AKQ43365.1, ECO:0000313|Proteomes:UP000059113};
RN [1] {ECO:0000313|EMBL:AKQ43365.1, ECO:0000313|Proteomes:UP000059113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113};
RX PubMed=26220886; DOI=10.1099/ijsem.0.000481;
RA Zhuang L., Liu Y., Wang L., Wang W., Shao Z.;
RT "Erythrobacter atlanticus sp. nov., a bacterium from ocean sediment able to
RT degrade polycyclic aromatic hydrocarbons.";
RL Int. J. Syst. Evol. Microbiol. 65:3714-3719(2015).
RN [2] {ECO:0000313|Proteomes:UP000059113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113};
RA Zhuang L., Liu Y., Shao Z.;
RT "The complete genome sequence of Erythrobacter sp. s21-N3.";
RL Submitted (APR-2015) 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; CP011310; AKQ43365.1; -; Genomic_DNA.
DR RefSeq; WP_048886919.1; NZ_CP011310.1.
DR AlphaFoldDB; A0A0H4VG43; -.
DR STRING; 1648404.CP97_10070; -.
DR KEGG; ery:CP97_10070; -.
DR PATRIC; fig|1648404.4.peg.2100; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000059113; 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; 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 Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Reference proteome {ECO:0000313|Proteomes:UP000059113};
KW Transferase {ECO:0000256|RuleBase:RU361137}.
FT DOMAIN 2..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 136..173
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 84..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 44203 MW; 867D9A04AA355FEA CRC64;
MPIAIKMPAL SPTMEEGTLA KWLVKVGDSV SAGDIMAEIE TDKATMEFEA VDEGVIAHIQ
VEEGAEGVAV GTVIATLAEE GEDAGSVAPI GSDDAAPAPT PAATESSSAP APTPAPTPAP
APSPSPAPAA SGDRIVASPL ARRIAEQEGV DLASVKGSGP NGRIVKADLE GAKLGATAPA
AAPSAATPAP AATAPAEAQD FGIPHEVEKL SGMRKTIARR LTESKQQIPH IYLTVDIRLD
ALLKLRSELN AALEPQGVKL SVNDLMIKAL GKSLEAVPAC NVQFAGDSLL RFKRADVSVA
VSIPNGLITP IISDAGNKAM SKISKEMKDL ASRAKEGKLA PEEYQGGTAS LSNMGMFGIS
QFSAVINPPQ AMIMAIGAGD KRPFVIDDTL QIASVMSATG SFDHRAIDGA DGAQLMKTFK
EMIEAPLGLV A
//
