ODP2_GEOSE
ID ODP2_GEOSE Reviewed; 428 AA.
AC P11961;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex;
DE EC=2.3.1.12;
DE AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE AltName: Full=E2;
GN Name=pdhC;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=2200674; DOI=10.1111/j.1432-1033.1990.tb19128.x;
RA Hawkins C.F., Borges A., Perham R.N.;
RT "Cloning and sequence analysis of the genes encoding the alpha and beta
RT subunits of the E1 component of the pyruvate dehydrogenase multienzyme
RT complex of Bacillus stearothermophilus.";
RL Eur. J. Biochem. 191:337-346(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-201.
RX PubMed=3421911; DOI=10.1042/bj2520079;
RA Packman L.C., Borges A., Perham R.N.;
RT "Amino acid sequence analysis of the lipoyl and peripheral subunit-binding
RT domains in the lipoate acetyltransferase component of the pyruvate
RT dehydrogenase complex from Bacillus stearothermophilus.";
RL Biochem. J. 252:79-86(1988).
RN [3]
RP STRUCTURE BY NMR OF 1-86.
RX PubMed=1915365; DOI=10.1111/j.1432-1033.1991.tb16275.x;
RA Dardel F., Laue E.D., Perham R.N.;
RT "Sequence-specific 1H-NMR assignments and secondary structure of the lipoyl
RT domain of the Bacillus stearothermophilus pyruvate dehydrogenase
RT multienzyme complex.";
RL Eur. J. Biochem. 201:203-209(1991).
RN [4]
RP STRUCTURE BY NMR OF 1-86, AND LIPOYLATION AT LYS-43.
RX PubMed=8445635; DOI=10.1006/jmbi.1993.1103;
RA Dardel F., Davis A.L., Laue E.D., Perham R.N.;
RT "Three-dimensional structure of the lipoyl domain from Bacillus
RT stearothermophilus pyruvate dehydrogenase multienzyme complex.";
RL J. Mol. Biol. 229:1037-1048(1993).
RN [5]
RP STRUCTURE BY NMR OF 129-171.
RX PubMed=8450544; DOI=10.1006/jmbi.1993.1145;
RA Kalia Y.N., Brocklehurst S.M., Hipps D.S., Appella E., Sakaguchi K.,
RA Perham R.N.;
RT "The high-resolution structure of the peripheral subunit-binding domain of
RT dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase
RT multienzyme complex of Bacillus stearothermophilus.";
RL J. Mol. Biol. 230:323-341(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 129-171.
RX PubMed=8805537; DOI=10.1016/s0969-2126(96)00032-9;
RA Mande S.S., Sarfaty S., Allen M.D., Perham R.N., Hol W.G.J.;
RT "Protein-protein interactions in the pyruvate dehydrogenase multienzyme
RT complex: dihydrolipoamide dehydrogenase complexed with the binding domain
RT of dihydrolipoamide acetyltransferase.";
RL Structure 4:277-286(1996).
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-
CC N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
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 -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Note=Binds 1 lipoyl cofactor covalently.;
CC -!- SUBUNIT: Forms a 60-polypeptide structural core with icosahedral
CC symmetry.
CC -!- INTERACTION:
CC P11961; P11959: pdhD; NbExp=3; IntAct=EBI-1040691, EBI-9021392;
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X53560; CAA37630.1; -; Genomic_DNA.
DR PIR; S10799; S14426.
DR RefSeq; WP_033016211.1; NZ_RCTK01000001.1.
DR PDB; 1B5S; X-ray; 4.40 A; A/B/C/D/E=185-426.
DR PDB; 1EBD; X-ray; 2.60 A; C=130-170.
DR PDB; 1LAB; NMR; -; A=2-81.
DR PDB; 1LAC; NMR; -; A=2-81.
DR PDB; 1W3D; NMR; -; A=119-171.
DR PDB; 1W4E; NMR; -; A=126-170.
DR PDB; 1W4F; NMR; -; A=126-170.
DR PDB; 1W4G; NMR; -; A=126-170.
DR PDB; 1W85; X-ray; 2.00 A; I/J=123-171.
DR PDB; 1W88; X-ray; 2.30 A; I/J=123-171.
DR PDB; 2PDD; NMR; -; A=129-171.
DR PDB; 2PDE; NMR; -; A=129-171.
DR PDB; 3DUF; X-ray; 2.50 A; I/J=1-428.
DR PDB; 3DV0; X-ray; 2.50 A; I/J=1-428.
DR PDB; 3DVA; X-ray; 2.35 A; I/J=1-428.
DR PDBsum; 1B5S; -.
DR PDBsum; 1EBD; -.
DR PDBsum; 1LAB; -.
DR PDBsum; 1LAC; -.
DR PDBsum; 1W3D; -.
DR PDBsum; 1W4E; -.
DR PDBsum; 1W4F; -.
DR PDBsum; 1W4G; -.
DR PDBsum; 1W85; -.
DR PDBsum; 1W88; -.
DR PDBsum; 2PDD; -.
DR PDBsum; 2PDE; -.
DR PDBsum; 3DUF; -.
DR PDBsum; 3DV0; -.
DR PDBsum; 3DVA; -.
DR AlphaFoldDB; P11961; -.
DR BMRB; P11961; -.
DR SMR; P11961; -.
DR DIP; DIP-6156N; -.
DR IntAct; P11961; 3.
DR PRIDE; P11961; -.
DR GeneID; 58572155; -.
DR BRENDA; 2.3.1.12; 623.
DR EvolutionaryTrace; P11961; -.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 4.10.320.10; -; 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 Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Direct protein sequencing; Glycolysis;
KW Lipoyl; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3421911"
FT CHAIN 2..428
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component of pyruvate dehydrogenase complex"
FT /id="PRO_0000162273"
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 130..167
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 88..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /evidence="ECO:0000255"
FT MOD_RES 43
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000269|PubMed:8445635"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1LAB"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1LAB"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1LAB"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1LAB"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1LAB"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1LAB"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1LAB"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:1W85"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:1W85"
SQ SEQUENCE 428 AA; 46326 MW; 2600CD150261ACB0 CRC64;
MAFEFKLPDI GEGIHEGEIV KWFVKPGDEV NEDDVLCEVQ NDKAVVEIPS PVKGKVLEIL
VPEGTVATVG QTLITLDAPG YENMTFKGQE QEEAKKEEKT ETVSKEEKVD AVAPNAPAAE
AEAGPNRRVI AMPSVRKYAR EKGVDIRLVQ GTGKNGRVLK EDIDAFLAGG AKPAPAAAEE
KAAPAAAKPA TTEGEFPETR EKMSGIRRAI AKAMVHSKHT APHVTLMDEA DVTKLVAHRK
KFKAIAAEKG IKLTFLPYVV KALVSALREY PVLNTSIDDE TEEIIQKHYY NIGIAADTDR
GLLVPVIKHA DRKPIFALAQ EINELAEKAR DGKLTPGEMK GASCTITNIG SAGGQWFTPV
INHPEVAILG IGRIAEKPIV RDGEIVAAPM LALSLSFDHR MIDGATAQKA LNHIKRLLSD
PELLLMEA
