ID A0A2S0MS25_9RHOB Unreviewed; 444 AA.
AC A0A2S0MS25;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=C6Y53_13920 {ECO:0000313|EMBL:AVO38680.1};
OS Pukyongiella litopenaei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pukyongiella.
OX NCBI_TaxID=2605946 {ECO:0000313|EMBL:AVO38680.1, ECO:0000313|Proteomes:UP000237655};
RN [1] {ECO:0000313|Proteomes:UP000237655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-1 {ECO:0000313|Proteomes:UP000237655};
RA Kim Y.-S., Kim S.-E., Kim K.-H.;
RT "Genomic analysis of the strain SH-1 isolated from shrimp intestine.";
RL Submitted (MAR-2018) 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:ARBA00000925,
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; CP027665; AVO38680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0MS25; -.
DR KEGG; thas:C6Y53_13920; -.
DR Proteomes; UP000237655; 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 GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:AVO38680.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237655};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361137}.
FT DOMAIN 2..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 137..174
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 90..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 45740 MW; 12E68946170C8D32 CRC64;
MATEILMPAL SPTMEEGTLA KWLVKEGDTV NSGDLLAEIE TDKATMEFEA VDEGVVGRIL
VAEGTEGVKV NSPIAILVEE GEEPGDIAAA PSAAAAPEAA QADTAAEAAP AGGSEKAAPP
APAPANAPVQ TGGARVFASP LARRIAAEKG LDLGAVKGSG PHGRIVRADV EGAIAAPVAT
PADAPAAAIS EAPAPVAALA AGPSADMVAR IYEDRNFDEV PLDGMRKTIA ARLTEAKQSI
PHFYLRRDIR LDALLAFRSQ LNRQLDARGV KLSVNDFIIK ACANALQAVP DANAVWAGDR
MLRLKPSDVA VAVAIEGGLF TPVLRDADTK SLSALSAEMK DLATRARDRK LAPHEYQGGS
FAISNLGMFG IDNFDAVINP PHGAILAVGA GVKKPVVGED GELAVATVMS VTLSVDHRVI
DGALGAKLLQ AIVDNLENPV VMLA
//