ID A3SJZ0_ROSNI Unreviewed; 429 AA.
AC A3SJZ0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=ISM_05240 {ECO:0000313|EMBL:EAP77671.1};
OS Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP77671.1, ECO:0000313|Proteomes:UP000005954};
RN [1] {ECO:0000313|EMBL:EAP77671.1, ECO:0000313|Proteomes:UP000005954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-591 / DSM 15170 / ISM
RC {ECO:0000313|Proteomes:UP000005954};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2005) 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:EAP77671.1}.
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DR EMBL; AALY01000001; EAP77671.1; -; Genomic_DNA.
DR AlphaFoldDB; A3SJZ0; -.
DR STRING; 89187.ISM_05240; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_2_5; -.
DR Proteomes; UP000005954; 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 Pyruvate {ECO:0000313|EMBL:EAP77671.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005954};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:EAP77671.1}.
FT DOMAIN 1..72
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 125..162
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 76..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 44553 MW; 694779A383CFB9BB CRC64;
MPALSPTMEE GTLAKWLVKE GDTVSSGDLL AEIETDKATM EFEAVDEGVI GKILVAEGSE
GVKVNTPIAV LLEEGESADD IGEASAPAAE PKAEAPKSDA APKPEAAPAA SAAPAAPKAD
GERIFASPLA RRIAADKGLD LSQISGSGPR GRIVKADVEN AQPSAAKPAA KDQPAAAPAA
AAPAATGPSS SQVIAMYEGR EYEEIPLNGM RKTIAARLTE AKQSIPHFYL RRDIRLDALL
KFRGQLNKQL EARSVKLSVN DFIIKACALA LQTVPAANAV WAGDRVLQLK PSDVAVAVAI
EGGLFTPVLK DAEMKSLSAL SSEMKDLASR ARDRKLAPHE YQGGSFAISN LGMFGIDNFD
AVINPPHGAI LAVGAGVKKP VVGADGELSV ATVMSVTLSV DHRVIDGALG AQLLDAIVQN
LENPMVMLA
//
