ID Q1PJX3_PROMR Unreviewed; 455 AA.
AC Q1PJX3;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=pdhC {ECO:0000313|EMBL:ABE11261.1};
GN ORFNames=HF10-88F10_0024 {ECO:0000313|EMBL:ABE11261.1};
OS uncultured Prochlorococcus marinus clone HF10-88F10.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=379378 {ECO:0000313|EMBL:ABE11261.1};
RN [1] {ECO:0000313|EMBL:ABE11261.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16556843; DOI=10.1126/science.1122050;
RA Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
RA Delong E.F., Chisholm S.W.;
RT "Genomic islands and the ecology and evolution of Prochlorococcus.";
RL Science 311:1768-1770(2006).
RN [2] {ECO:0000313|EMBL:ABE11261.1}
RP NUCLEOTIDE SEQUENCE.
RG US DOE Joint Genome Institute (JGI);
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Richardson P.;
RT "Sequencing of the draft fosmids and assembly of Prochlorococcus marinus
RT environmental genome fragment.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; DQ366726; ABE11261.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1PJX3; -.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:RHEA.
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; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF75; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT 5 OF PYRUVATE DEHYDROGENASE COMPLEX, CHLOROPLASTIC; 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:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ABE11261.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 156..193
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 87..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 48745 MW; EABEACA0AD5943DB CRC64;
MSHEIFMPAL SSTMTEGKIV EWLKNPGDKV ERGESVLVVE SDKADMDVES FQDGYLAAVL
MPAGSTAPVG ETIGLIVENE DEIASVQEQN KGNQPEVSTS DQLELVSNKT EEKPVVQTKN
INKEAEEVVL KSEKPAPIFN SDQINAATSN VSSRVIASPR AKKLASQMGV DLAKVHGSGP
HGRIQADDIL KANGQPVSIP WIGEGGSPAS IPGANLGVES KPETSGNSFG NPGETVQFNT
LQKAVNKNME SSLDVPCFRV GYSINTDKLD NFYKKVKQNG VTMTALLVKA VAKTLKKHPQ
VNSSFSENGI SYPENINIAV AVAMEDGGLI TPVLKEPCNT DLFELSREWK DLVKRSRSKQ
LEPDEYSTGT FTLSNLGMFG VDRFDAILPP GTGAILAIAS SKPTVVANSD GSISVKKIMQ
VNLTADHRVI YGADGASFLK DLASLIEDEP ETLVS
//
