ID A0A290Q1J3_9BACT Unreviewed; 443 AA.
AC A0A290Q1J3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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 ORFNames=CMV30_00085 {ECO:0000313|EMBL:ATC62499.1};
OS Nibricoccus aquaticus.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Nibricoccus.
OX NCBI_TaxID=2576891 {ECO:0000313|EMBL:ATC62499.1, ECO:0000313|Proteomes:UP000217265};
RN [1] {ECO:0000313|EMBL:ATC62499.1, ECO:0000313|Proteomes:UP000217265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ-65 {ECO:0000313|EMBL:ATC62499.1,
RC ECO:0000313|Proteomes:UP000217265};
RA Choi A.;
RT "Complete genome sequence of Verrucomicrobial strain HZ-65, isolated from
RT freshwater.";
RL Submitted (SEP-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 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; CP023344; ATC62499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A290Q1J3; -.
DR KEGG; vbh:CMV30_00085; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000217265; 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; 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; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:ATC62499.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217265};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:ATC62499.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 144..181
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 84..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 45892 MW; 82A5B1A76F4BDD93 CRC64;
MAQIIEMPKL SDTMTVGTLV KWLKKEGDVI TAGTMLAEVE TDKATMELEC FYDGTLLKIF
APAGTQLAIG APLCAVGKPG ENVEAPAGKP ASPAAAKEEP KKDAPKSESA PAPAKAPESV
PQPETKPAAA AHSAPARADG ERVKISPLAK KLAAEKGIDP SRVTGSGPGG RIVRADVLAA
EKSGSAKAGS AKPAATGAPS TPFTGGAVSR TGPIQEERAV PVSNMRAVIA KRMVESTTTI
PYIYVDIEID AEPLLAVRQQ LNTGLEKEGV KLSVNDFVLK ACAEALRRVP AVNSSWEGNQ
IRYFGAAHVA FAVALDDGLI TPVVKDAHQK SVFQISIEAK ALGKKAKDKK LAPAEYTGGT
FCVSNLGMMG IPKFTAIINP PNSAILAVGA AVAKPVIKNG QIVSGQTMTV TLSGDHRVFD
GAVGAQFLNA LKTLIESPAL LLV
//
