ID A0A2I0FVA6_9GAMM Unreviewed; 627 AA.
AC A0A2I0FVA6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=aceF {ECO:0000313|EMBL:PKH22747.1};
GN ORFNames=CIG19_12275 {ECO:0000313|EMBL:PKH22747.1};
OS Enterobacterales bacterium CwR94.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales.
OX NCBI_TaxID=2025587 {ECO:0000313|EMBL:PKH22747.1, ECO:0000313|Proteomes:UP000237543};
RN [1] {ECO:0000313|EMBL:PKH22747.1, ECO:0000313|Proteomes:UP000237543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CwR94 {ECO:0000313|EMBL:PKH22747.1,
RC ECO:0000313|Proteomes:UP000237543};
RA de Groot N.N.;
RL Submitted (AUG-2017) 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 3 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 ECO:0000256|RuleBase:RU361137}.
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:PKH22747.1}.
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DR EMBL; NVXY01000009; PKH22747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0FVA6; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000237543; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 3.
DR Gene3D; 2.40.50.100; -; 3.
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; IPR006256; AcTrfase_Pyrv_DH_cplx.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01348; PDHac_trf_long; 1.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 3.
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; 3.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR PROSITE; PS00189; LIPOYL; 3.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361137,
KW ECO:0000313|EMBL:PKH22747.1};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:PKH22747.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237543};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:PKH22747.1}.
FT DOMAIN 2..75
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 105..178
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 204..277
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 325..362
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 84..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 65822 MW; 88B9A8AC0812584A CRC64;
MAIEINVPDI GADEVEVTEV MVKVGDKVEV EQSLISVEGD KASMEVPSPQ AGVVKEIKVA
VGDKVETGKL IMIFEAEGAT AAAPAQAEEK KEAAPAASAP AAAESKEVNV PDIGGDEVEV
TEIMVKVGDT VEAEQSLLTV EGDKASMEVP APFAGTVKEI KISTGDKVST GSLIMVFEVA
GSGAAPAAKQ EAAPAPAAPV AAGSKDVNVP DIGGDEVEIT EVMVKVGDKV AAEQSLITVE
GDKASMEVPA PFAGTVKEIK ISTGDKVSTG SLIMVFEVEG AAPTAAPAAK QEAAPAKAEQ
KAAPAAAPAK AAGKDEFAEN DAYVHATPVI RRLAREFGVN LAKVKGSGRK GRILKEDVQA
YVKDAVKRAE TAPAATGGGL PGMLPWPKVD FSKFGEIEEV ELGRIQKISG ANLSRNWVMI
PHVTHFDKTD ITELEAFRKQ QNAEAEKRKL DVKFTPVVFI MKAVAAALEQ MPRFNSSLSE
DGQKLTLKKY INIGVAVDTP NGLVVPVFKD VNKKGITELS RELMAISKKA RDGKLTASDM
QGGCFTISSL GGLGTTHFTP IVNAPEVAIL GVSKSAMEPV WNGKEFAPRL MMPISLSFDH
RVIDGADGAR FITIIGNTLA DIRRLVM
//
