ODO2_STAHJ
ID ODO2_STAHJ Reviewed; 423 AA.
AC Q4L6C3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=odhB; Synonyms=sucB; OrderedLocusNames=SH1493;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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). {ECO:0000250|UniProtKB:P0AFG6}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AP006716; BAE04802.1; -; Genomic_DNA.
DR RefSeq; WP_011275788.1; NC_007168.1.
DR AlphaFoldDB; Q4L6C3; -.
DR SMR; Q4L6C3; -.
DR STRING; 279808.SH1493; -.
DR PRIDE; Q4L6C3; -.
DR EnsemblBacteria; BAE04802; BAE04802; SH1493.
DR GeneID; 58062304; -.
DR KEGG; sha:SH1493; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_0_0_9; -.
DR OMA; MKVPSPG; -.
DR OrthoDB; 1626282at2; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000000543; 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 3: Inferred from homology;
KW Acyltransferase; Lipoyl; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..423
FT /note="Dihydrolipoyllysine-residue succinyltransferase
FT component of 2-oxoglutarate dehydrogenase complex"
FT /id="PRO_0000288109"
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 128..164
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 74..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 394
FT /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT ACT_SITE 398
FT /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT MOD_RES 42
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
SQ SEQUENCE 423 AA; 46249 MW; C1FD7CF93C4E1D88 CRC64;
MPEVKVPELA ESITEGTIAE WLKNVGDSVE KGEAILELET DKVNVEVVSE EEGVLQEQLA
SEGDTVEVGQ VIATVGEGSG NASSSKEESS DQSQSANNDE ATKELAQPTE SQSNNEETQS
NPNNQRVNAT PSARRHAREN GVDLSTVSGK GNDVVRKDDV ENSQKAAQSQ SSQETSKKEE
PKKSSGAPNK PVIREKMSRR KKTAAKKLLE VSNNTAMLTT FNEVDMTNVM ELRKRKKEQF
IKDHDGTKLG FMSFFTKAAV AALKKYPEVN AEIDGDDMIT KQYYDIGVAV STDDGLLVPF
VRDCDKKNFA ELERAIADLA VKARDKKLGL DDMVNGSFTI TNGGVFGSMM STPIINGNQA
AILGMHSIIT RPIAIDKDTI ENRPMMYIAL SYDHRIIDGK EAVGFLKTIK ELIESPEDLL
LES
