ID ODP2_CORGL Reviewed; 675 AA.
AC Q8NNJ2; Q6M3N0;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, 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=Pyruvate dehydrogenase complex component E2;
DE Short=PDH component E2;
GN Name=aceF; Synonyms=sucB; OrderedLocusNames=Cgl2207, cg2421;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP IDENTIFICATION IN THE ODH/PDH COMPLEX.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16522631; DOI=10.1074/jbc.m512515200;
RA Niebisch A., Kabus A., Schultz C., Weil B., Bott M.;
RT "Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase
RT activity via the phosphorylation status of the OdhI protein.";
RL J. Biol. Chem. 281:12300-12307(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, COFACTOR, LIPOYLATION
RP AT LYS-43; LYS-162 AND LYS-278, AND MUTAGENESIS OF LYS-43; LYS-162 AND
RP LYS-278.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=20675489; DOI=10.1128/jb.00597-10;
RA Hoffelder M., Raasch K., van Ooyen J., Eggeling L.;
RT "The E2 domain of OdhA of Corynebacterium glutamicum has
RT succinyltransferase activity dependent on lipoyl residues of the
RT acetyltransferase AceF.";
RL J. Bacteriol. 192:5203-5211(2010).
CC -!- FUNCTION: Is essential for both 2-oxoglutarate dehydrogenase (ODH) and
CC pyruvate dehydrogenase (PDH) activities, but AceF has exclusively
CC transacetylase (and no transsuccinylase) activity. The lipoyl residues
CC required for ODH activity are likely provided by AceF.
CC {ECO:0000269|PubMed:20675489}.
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:0000269|PubMed:20675489};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000305|PubMed:20675489};
CC Note=Binds 3 lipoyl cofactors covalently.
CC {ECO:0000305|PubMed:20675489};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry (By similarity). Part of an unusual ODH/PDH supercomplex,
CC consisting of AceE (E1), AceF (E2), and Lpd (E3) together with OdhA
CC (E1+E2). {ECO:0000250, ECO:0000269|PubMed:16522631}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display no ODH and no PDH
CC activities. {ECO:0000269|PubMed:20675489}.
CC -!- MISCELLANEOUS: Is the only lipoylated protein in C.glutamicum.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; BA000036; BAB99600.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20547.1; -; Genomic_DNA.
DR RefSeq; NP_601410.1; NC_003450.3.
DR RefSeq; WP_011014958.1; NC_006958.1.
DR PDB; 6ZZI; X-ray; 1.93 A; A/B/C/D/E/F=437-675.
DR PDB; 6ZZJ; X-ray; 1.35 A; A=437-675.
DR PDB; 6ZZK; X-ray; 2.09 A; A/B=437-675.
DR PDB; 6ZZL; X-ray; 2.23 A; A/B/C=367-675.
DR PDBsum; 6ZZI; -.
DR PDBsum; 6ZZJ; -.
DR PDBsum; 6ZZK; -.
DR PDBsum; 6ZZL; -.
DR AlphaFoldDB; Q8NNJ2; -.
DR SMR; Q8NNJ2; -.
DR STRING; 196627.cg2421; -.
DR KEGG; cgb:cg2421; -.
DR KEGG; cgl:Cgl2207; -.
DR PATRIC; fig|196627.13.peg.2142; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_1_11; -.
DR OrthoDB; 9805770at2; -.
DR BioCyc; CORYNE:G18NG-11799-MONOMER; -.
DR BRENDA; 1.2.1.104; 960.
DR BRENDA; 1.2.1.105; 960.
DR BRENDA; 2.3.1.61; 960.
DR SABIO-RK; Q8NNJ2; -.
DR Proteomes; UP000000582; Chromosome.
DR Proteomes; UP000001009; 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 GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 3.
DR Gene3D; 2.40.50.100; -; 3.
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; IPR014276; 2-oxoglutarate_DH_E2.
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 NCBIfam; TIGR02927; SucB_Actino; 1.
DR PANTHER; PTHR43416:SF8; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 3.
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; 3.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR PROSITE; PS00189; LIPOYL; 3.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Lipoyl; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..675
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component of pyruvate dehydrogenase complex"
FT /id="PRO_0000420521"
FT DOMAIN 2..77
FT /note="Lipoyl-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 121..196
FT /note="Lipoyl-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 237..312
FT /note="Lipoyl-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 372..409
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 77..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 645
FT /evidence="ECO:0000250"
FT ACT_SITE 649
FT /evidence="ECO:0000250"
FT MOD_RES 43
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000305|PubMed:20675489"
FT MOD_RES 162
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000305|PubMed:20675489"
FT MOD_RES 278
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000305|PubMed:20675489"
FT MUTAGEN 43
FT /note="K->Q: No effect on ODH and PDH activity; when
FT associated with Q-162."
FT /evidence="ECO:0000269|PubMed:20675489"
FT MUTAGEN 162
FT /note="K->Q: No effect on ODH and PDH activity; when
FT associated with Q-43. Strong reduction in the catalytic
FT efficiency of ODH and slight reduction in that of PDH; when
FT associated with Q-278."
FT /evidence="ECO:0000269|PubMed:20675489"
FT MUTAGEN 278
FT /note="K->Q: Strong reduction in the catalytic efficiency
FT of ODH and slight reduction in that of PDH; when associated
FT with Q-162."
FT /evidence="ECO:0000269|PubMed:20675489"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:6ZZL"
FT HELIX 432..436
FT /evidence="ECO:0007829|PDB:6ZZL"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:6ZZL"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:6ZZI"
FT HELIX 446..460
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT STRAND 464..472
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT HELIX 474..491
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT HELIX 498..511
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT TURN 513..515
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT TURN 521..524
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:6ZZI"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:6ZZI"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT HELIX 557..572
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT HELIX 578..581
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT STRAND 585..589
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT HELIX 591..594
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT STRAND 617..625
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT STRAND 628..644
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT TURN 645..647
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT HELIX 650..666
FT /evidence="ECO:0007829|PDB:6ZZJ"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:6ZZJ"
SQ SEQUENCE 675 AA; 70905 MW; 1D262FA89899B47F CRC64;
MAFSVEMPEL GESVTEGTIT QWLKSVGDTV EVDEPLLEVS TDKVDTEIPS PVAGVILEIK
AEEDDTVDVG GVIAIIGDAD ETPANEAPAD EAPAPAEEEE PVKEEPKKEA APEAPAATGA
ATDVEMPELG ESVTEGTITQ WLKAVGDTVE VDEPLLEVST DKVDTEIPSP VAGTIVEILA
DEDDTVDVGA VIARIGDANA AAAPAEEEAA PAEEEEPVKE EPKKEAAPEA PAATGAATDV
EMPELGESVT EGTITQWLKA VGDTVEVDEP LLEVSTDKVD TEIPSPVAGT IVEILADEDD
TVDVGAVIAR IGDANAAAAP AEEEAAPAEE EEPVKEEPKK EEPKKEEPKK EAATTPAAAS
ATVSASGDNV PYVTPLVRKL AEKHGVDLNT VTGTGIGGRI RKQDVLAAAN GEAAPAEAAA
PVSAWSTKSV DPEKAKLRGT TQKVNRIREI TAMKTVEALQ ISAQLTQLHE VDMTRVAELR
KKNKPAFIEK HGVNLTYLPF FVKAVVEALV SHPNVNASFN AKTKEMTYHS SVNLSIAVDT
PAGLLTPVIH DAQDLSIPEI AKAIVDLADR SRNNKLKPND LSGGTFTITN IGSEGALSDT
PILVPPQAGI LGTGAIVKRP VVITEDGIDS IAIRQMVFLP LTYDHQVVDG ADAGRFLTTI
KDRLETANFE GDLQL
//
