ID D5SV60_PLAL2 Unreviewed; 425 AA.
AC D5SV60;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN OrderedLocusNames=Plim_3533 {ECO:0000313|EMBL:ADG69346.1};
OS Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS (Planctomyces limnophilus).
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctopirus.
OX NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG69346.1, ECO:0000313|Proteomes:UP000002220};
RN [1] {ECO:0000313|EMBL:ADG69346.1, ECO:0000313|Proteomes:UP000002220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290
RC {ECO:0000313|Proteomes:UP000002220};
RX PubMed=21304691; DOI=10.4056/sigs.1052813;
RA Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT 290).";
RL Stand. Genomic Sci. 3:47-56(2010).
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001744; ADG69346.1; -; Genomic_DNA.
DR RefSeq; WP_013111777.1; NC_014148.1.
DR AlphaFoldDB; D5SV60; -.
DR STRING; 521674.Plim_3533; -.
DR KEGG; plm:Plim_3533; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_0; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000002220; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
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; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
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; 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 Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000002220};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 133..170
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 81..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 44378 MW; AC51ED8D74488FE6 CRC64;
MSVEFKLPQL AEGIDSADIA QILVSAGDTI EAGKIVMELE TDKAVMELAC PHAGKIGKIH
VKPGETIKTG QLLLSIEASG ASNGTSAKPA SPAASSSAPA APAKATPAAP VKAAPAPAAV
AAPTRSTVEI PIAAGPATRR LARELGMQLE RLRGTGPGGR ITQEDVARAY AAQQGGGGGG
VVAPPLPDFS QYGPITAQAL TKLQKTSANN LSAAWQLIPH VTQHDLADIT ETESARKRFQ
EAVAKGGPKV TMTAVAMKAA VAALKAFPNF NSSIDMSRGE VILKSYYNIG IAVDTPNGLV
VPVVRDVDKK SILQLATELT EIAEKARNRK LEIKDMQGGT FTITNLGGIG GTAFTPIVNY
PEVAILGMSR SFHQLQLVDG QVKERLMLPL SLSYDHRVVN GADAARFVVK LTSLLSDAFK
LLVEC
//
