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Database: UniProt
Entry: A0A220RZP8_9NEIS
LinkDB: A0A220RZP8_9NEIS
Original site: A0A220RZP8_9NEIS 
ID   A0A220RZP8_9NEIS        Unreviewed;       381 AA.
AC   A0A220RZP8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
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:ROV56329.1};
GN   ORFNames=BG910_01930 {ECO:0000313|EMBL:ASK26667.1}, EGS38_04740
GN   {ECO:0000313|EMBL:ROV56329.1};
OS   Neisseria chenwenguii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=1853278 {ECO:0000313|EMBL:ASK26667.1, ECO:0000313|Proteomes:UP000198238};
RN   [1] {ECO:0000313|EMBL:ASK26667.1, ECO:0000313|Proteomes:UP000198238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10023 {ECO:0000313|EMBL:ASK26667.1,
RC   ECO:0000313|Proteomes:UP000198238};
RA   Zhang G.;
RT   "Neisseria chenwenguii sp. nov., isolated from the intestinal contents of
RT   Tibetan Plateau Pika in Yushu, Qinghai Province, China.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ROV56329.1, ECO:0000313|Proteomes:UP000270353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10010 {ECO:0000313|EMBL:ROV56329.1,
RC   ECO:0000313|Proteomes:UP000270353};
RA   Zhang G.;
RT   "Neisseria chenwenguii sp. nov. isolated from the rectal contents of
RT   plateau pika (Ochotona cruzoniae).";
RL   Submitted (NOV-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   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361138}.
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DR   EMBL; CP022278; ASK26667.1; -; Genomic_DNA.
DR   EMBL; RKIL01000007; ROV56329.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A220RZP8; -.
DR   KEGG; nei:BG910_01930; -.
DR   OrthoDB; 9805770at2; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000198238; Chromosome.
DR   Proteomes; UP000270353; 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; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 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   Reference proteome {ECO:0000313|Proteomes:UP000198238};
KW   Transferase {ECO:0000256|RuleBase:RU361138, ECO:0000313|EMBL:ASK26667.1};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          96..133
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   381 AA;  40581 MW;  C0B0E18A51DC21DA CRC64;
     MIVEVKVPML SESVSEGTLL EWKKQVGEAV ARDEILIDIE TDKVVLEVPA PQAGVLVEIV
     AQNGETVAAD QVLARIDTAA AAEAAPAAAN VSAQAGVMPA AAKLAAENGV DTANLQGSGR
     GGRVLKEDVQ NAGKPAAAAA APNPVLNGDR PEQRVPMSRL RARVAERLLA SQQENAILTT
     FNEVNMKPVM DLRNKYKEKF EKEHGVKLGF MSFFVKAAVA ALKKFPVVNA SVDGSDIVYH
     GYFDIGIAIG SPRGLVVPIL RDADRMSIAD IEKAIVDYAV KAKDGKIALE DLTGGTFSIT
     NGGTFGSMMS TPIINPPQSA ILGMHATKER AVVENGQVVV RPMMYLALSY DHRIIDGREA
     VLTLVTIKDL LEDPARLLLD L
//
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