ODO2_ECO57
ID ODO2_ECO57 Reviewed; 405 AA.
AC P0AFG7; P07016;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE EC=2.3.1.61 {ECO:0000250|UniProtKB:P0AFG6};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2;
DE Short=OGDC-E2;
DE AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
GN Name=sucB; OrderedLocusNames=Z0881, ECs0752;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: E2 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the second step in the conversion of 2-
CC oxoglutarate to succinyl-CoA and CO(2). {ECO:0000250|UniProtKB:P0AFG6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-
CC succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581,
CC Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000250|UniProtKB:P0AFG6};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 6/6.
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. Part of the 2-oxoglutarate dehydrogenase (OGDH) complex
CC composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide
CC succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the
CC complex contains multiple copies of the three enzymatic components (E1,
CC E2 and E3). Interacts with SucA (via N-terminus), the E1 component of
CC OGDH complex. {ECO:0000250|UniProtKB:P0AFG6}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG55051.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34175.1; -; Genomic_DNA.
DR PIR; G85573; G85573.
DR PIR; H90722; H90722.
DR RefSeq; NP_308779.1; NC_002695.1.
DR RefSeq; WP_000099823.1; NZ_SWKA01000005.1.
DR PDB; 2CYU; NMR; -; A=113-152.
DR PDBsum; 2CYU; -.
DR AlphaFoldDB; P0AFG7; -.
DR BMRB; P0AFG7; -.
DR SMR; P0AFG7; -.
DR STRING; 155864.EDL933_0796; -.
DR EnsemblBacteria; AAG55051; AAG55051; Z0881.
DR EnsemblBacteria; BAB34175; BAB34175; ECs_0752.
DR GeneID; 58460903; -.
DR GeneID; 917484; -.
DR KEGG; ece:Z0881; -.
DR KEGG; ecs:ECs_0752; -.
DR PATRIC; fig|386585.9.peg.870; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_0_0_6; -.
DR OMA; MKVPSPG; -.
DR UniPathway; UPA00868; UER00840.
DR EvolutionaryTrace; P0AFG7; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
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; 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 InterPro; IPR006255; SucB.
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 TIGRFAMs; TIGR01347; sucB; 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; Acetylation; Acyltransferase; Lipoyl; Reference proteome;
KW Transferase; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..405
FT /note="Dihydrolipoyllysine-residue succinyltransferase
FT component of 2-oxoglutarate dehydrogenase complex"
FT /id="PRO_0000162263"
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 113..150
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 75..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 376
FT /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT ACT_SITE 380
FT /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT MOD_RES 44
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:2CYU"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2CYU"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2CYU"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:2CYU"
SQ SEQUENCE 405 AA; 44011 MW; 8439E48C6D381277 CRC64;
MSSVDILVPD LPESVADATV ATWHKKPGDA VVRDEVLVEI ETDKVVLEVP ASADGILDAV
LEDEGTTVTS RQILGRLREG NSAGKETSAK SEEKASTPAQ RQQASLEEQN NDALSPAIRR
LLAEHNLDAS AIKGTGVGGR LTREDVEKHL AKAPAKESAP AAAAPAAQPA LAARSEKRVP
MTRLRKRVAE RLLEAKNSTA MLTTFNEVNM KPIMDLRKQY GEAFEKRHGI RLGFMSFYVK
AVVEALKRYP EVNASIDGDD VVYHNYFDVS MAVSTPRGLV TPVLRDVDTL GMADIEKKIK
ELAVKGRDGK LTVEDLTGGN FTITNGGVFG SLMSTPIINP PQSAILGMHA IKDRPMAVNG
QVEILPMMYL ALSYDHRLID GRESVGFLVT IKELLEDPTR LLLDV
