ODP2_CUPNH
ID ODP2_CUPNH Reviewed; 553 AA.
AC Q59098; Q0KBW0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 138.
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=pdhB; OrderedLocusNames=H16_A1375;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8021225; DOI=10.1128/jb.176.14.4394-4408.1994;
RA Hein S., Steinbuechel A.;
RT "Biochemical and molecular characterization of the Alcaligenes eutrophus
RT pyruvate dehydrogenase complex and identification of a new type of
RT dihydrolipoamide dehydrogenase.";
RL J. Bacteriol. 176:4394-4408(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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; Evidence={ECO:0000250};
CC Note=Binds 2 lipoyl cofactors covalently. {ECO:0000250};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA21599.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U09865; AAA21599.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AM260479; CAJ92511.1; -; Genomic_DNA.
DR PIR; B55514; B55514.
DR RefSeq; WP_011615028.1; NC_008313.1.
DR AlphaFoldDB; Q59098; -.
DR SMR; Q59098; -.
DR STRING; 381666.H16_A1375; -.
DR EnsemblBacteria; CAJ92511; CAJ92511; H16_A1375.
DR KEGG; reh:H16_A1375; -.
DR PATRIC; fig|381666.6.peg.1764; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_4; -.
DR OMA; TMEFESF; -.
DR OrthoDB; 1626282at2; -.
DR Proteomes; UP000008210; Chromosome 1.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
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; IPR006256; AcTrfase_Pyrv_DH_cplx.
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:SF2; PTHR43178:SF2; 3.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 2.
DR TIGRFAMs; TIGR01348; PDHac_trf_long; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Glycolysis; Lipoyl; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..553
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component of pyruvate dehydrogenase complex"
FT /id="PRO_0000162271"
FT DOMAIN 4..78
FT /note="Lipoyl-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 122..196
FT /note="Lipoyl-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 250..287
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 97..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 526
FT /evidence="ECO:0000255"
FT MOD_RES 44
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT MOD_RES 162
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 201
FT /note="S -> A (in Ref. 1; AAA21599)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="F -> V (in Ref. 1; AAA21599)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 56582 MW; 280424CA0475D9E3 CRC64;
MSQAIEIKVP DIGDYDAVPV IEVHVKPGDS INAEDALVTL ESDKATMDVP SPQAGVVKDV
RIKVGDNVSE GSVLVMLEAA NEPAAAPAPA AAAPAPAAAA PAPAPAPAAA PAAAPAAGGG
GTIEVKVPDI GDYDAVPVIE VHVKAGDTIN AEDAVVTLES DKATMDVPSP QGGVVKEVKV
KVGDNVAEGT LLLILEGAAA SAAPAAAAAA PAPAASAPAP APAPAAAAPA PAAAPAAAPA
AAGVTGKAAH ASPSVRKFAR ELGVDVSRVP GTGPKGRITQ EDVQGYVKGV MSGQAAAPAQ
AAAAGAGGGE LGLLPWPKFD FTRFGEVESK ALSRIKKISG ANLHRNWVMI PHVTNHDEAD
ITELEAFRLQ LNKENEKSGI KVTMLAFMIK ATVAALKKFP NFNASLDGDN LVLKKYFNIG
FAADTPNGLV VPVIKDADKK GVLEISQEMS ELAKLARDGK LKPDQMQGGC FSISSLGGLG
GTYFTPIINA PEVAIMGVCK SYQKPVWDGK QFAPRLTLPL SLSWDHRVID GAEAARFNTY
FGQLLADFRR ILL
