ID A0A291JJN7_9STAP Unreviewed; 427 AA.
AC A0A291JJN7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|ARBA:ARBA00019511, ECO:0000256|RuleBase:RU361138};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945, ECO:0000256|RuleBase:RU361138};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|RuleBase:RU361138};
GN Name=odhB {ECO:0000313|EMBL:SUM55142.1};
GN Synonyms=sucB {ECO:0000313|EMBL:PNZ95152.1};
GN ORFNames=BJD96_07200 {ECO:0000313|EMBL:ATH60101.1}, BUZ61_01235
GN {ECO:0000313|EMBL:PTK60732.1}, CD130_12410
GN {ECO:0000313|EMBL:PNZ95152.1}, NCTC13834_01501
GN {ECO:0000313|EMBL:SUM55142.1};
OS Staphylococcus nepalensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=214473 {ECO:0000313|EMBL:ATH60101.1, ECO:0000313|Proteomes:UP000217956};
RN [1] {ECO:0000313|EMBL:PTK60732.1, ECO:0000313|Proteomes:UP000240400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNUC 4337 {ECO:0000313|EMBL:PTK60732.1,
RC ECO:0000313|Proteomes:UP000240400};
RX PubMed=28066335; DOI=.3389/fmicb.2016.01990;
RA Naushad S., Barkema H.W., Luby C., Condas L.A., Nobrega D.B., Carson D.A.,
RA De Buck J.;
RT "Comprehensive Phylogenetic Analysis of Bovine Non-aureus Staphylococci
RT Species Based on Whole-Genome Sequencing.";
RL Front. Microbiol. 7:1990-1990(2016).
RN [2] {ECO:0000313|EMBL:ATH60101.1, ECO:0000313|Proteomes:UP000217956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1 {ECO:0000313|EMBL:ATH60101.1,
RC ECO:0000313|Proteomes:UP000217956};
RA Nam Y.-D., Kang J., Chung W.-H.;
RT "Complete genome sequence of Staphylococcus nepalensis JS1.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PNZ95152.1, ECO:0000313|Proteomes:UP000236280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15150 {ECO:0000313|EMBL:PNZ95152.1,
RC ECO:0000313|Proteomes:UP000236280};
RA Cole K., Golubchik T., Russell J., Foster D., Llewelyn M., Wilson D.,
RA Crook D., Paul J.;
RT "Draft genome sequences of 64 type strains of genus Staph aureus.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:PTK60732.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SNUC 4337 {ECO:0000313|EMBL:PTK60732.1};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:SUM55142.1, ECO:0000313|Proteomes:UP000254412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13834 {ECO:0000313|EMBL:SUM55142.1,
RC ECO:0000313|Proteomes:UP000254412};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00004052,
CC ECO:0000256|RuleBase:RU361138}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000256|ARBA:ARBA00043693,
CC ECO:0000256|RuleBase:RU361138};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU361138};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000256|RuleBase:RU361138};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 6/6.
CC {ECO:0000256|ARBA:ARBA00005145, ECO:0000256|RuleBase:RU361138}.
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:0000256|ARBA:ARBA00011666}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361138}.
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DR EMBL; CP017460; ATH60101.1; -; Genomic_DNA.
DR EMBL; PPRR01000274; PNZ95152.1; -; Genomic_DNA.
DR EMBL; PZHR01000003; PTK60732.1; -; Genomic_DNA.
DR EMBL; UHDS01000001; SUM55142.1; -; Genomic_DNA.
DR KEGG; snl:BJD96_07200; -.
DR OrthoDB; 9805770at2; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000217956; Chromosome.
DR Proteomes; UP000236280; Unassembled WGS sequence.
DR Proteomes; UP000240400; Unassembled WGS sequence.
DR Proteomes; UP000254412; Unassembled WGS sequence.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
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; 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 NCBIfam; TIGR01347; sucB; 1.
DR PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 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; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU361138};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361138};
KW Transferase {ECO:0000256|RuleBase:RU361138, ECO:0000313|EMBL:ATH60101.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU361138}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 129..165
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 75..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 46762 MW; ED394E9707244B0B CRC64;
MPEVKVPELA ESITEGTIAE WLKQVGDSVD KGEAILELET DKVNVEVVSE EAGVLQELLA
NEGDTVEVGQ SIAVVGEGSG NNAPETSKQD DSEKQSSASS NENEANQTKS EPQNDSASDN
AQDKGARVNA TPSARKYARE KGIDLSEVAT QSNDIVRKEH VNQTQNNQSN SQQTAQSSTK
EEPKKTAAQQ NPTKPVIREK MSRRKKTAAK KLLEVSNNTA MLTTFNEIDM TNVMNLRKRK
KEQFIKDHDG TKLGFMSFFT KAAVAALKKY PEVNAEIDGE DMITKQFYDI GVAVSTEDGL
LVPFVRDCDK KNFAEIEDEI ANLATKARDK KLGLDDMVNG SFTITNGGIF GSMMSTPIIN
GSQAAILGMH SIITRPIAID ADTIENRPMM YIALSYDHRI IDGKEAVGFL KTIKELIENP
EDLLLES
//
