ID A0A0W1DVI3_9SPHN Unreviewed; 444 AA.
AC A0A0W1DVI3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=ATE67_05645 {ECO:0000313|EMBL:KTE22104.1};
OS Sphingopyxis sp. H050.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1759072 {ECO:0000313|EMBL:KTE22104.1, ECO:0000313|Proteomes:UP000053439};
RN [1] {ECO:0000313|Proteomes:UP000053439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H050 {ECO:0000313|Proteomes:UP000053439};
RA Gomez-Alvarez V., Revetta R.P.;
RL Submitted (NOV-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}.
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:KTE22104.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNRZ01000002; KTE22104.1; -; Genomic_DNA.
DR RefSeq; WP_058815630.1; NZ_LNRZ01000002.1.
DR AlphaFoldDB; A0A0W1DVI3; -.
DR STRING; 1759072.ATE67_05645; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000053439; 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; 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 Transferase {ECO:0000256|RuleBase:RU361137}.
FT DOMAIN 2..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 141..178
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 105..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 45223 MW; 9903750D7DD6D119 CRC64;
MPIELKMPAL SPTMEEGTLA KWLVKEGDAV KSGDLLAEIE TDKATMEFEA IDEGVVRQIL
VPEGTDGVKV GTVIAVIAGE GEDASSAKAA PAAISPAPVE TKDVAPAKAG AASNSAPTPA
APAFAGATEK AAPVASGDRI KASPLAKRLA AERGIDLSTI KGTGPGGRIV KDDLEGAPAG
TAAPAATAAP AAAAPAAAPA AAPAPVAAGP IPDFGIPHED EKLSGMRKTI ARRLSQSMQE
SPHIYLTVDI RLDALLKLRG ELNASLEGRG VKLSVNDMLI KALAVALERV PSCNVSFGGD
VMRFYKRADI SVAVSIPGGL ITPIIVDAGG KSMSKISTEM AELAAKAKEG KLQPSEYQGG
TASISNMGMM GIKQFTAVIN PPQAMIMAIG AGEKRPYVVD DALAIATVMS ATGSFDHRAI
DGADGALLMK TFKELVESPL GLVA
//
