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ODP2_CORGL
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   03-AUG-2022, entry version 130.
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; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   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=(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         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   OMA; MKVPSPG; -.
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   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   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; 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   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 3.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 3.
DR   TIGRFAMs; TIGR02927; SucB_Actino; 1.
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; Glycolysis; Lipoyl; Reference proteome;
KW   Repeat; Transferase; Tricarboxylic acid cycle.
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
 
 
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