ID A0A0P7VLS9_9RHOB Unreviewed; 480 AA.
AC A0A0P7VLS9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=sucB {ECO:0000313|EMBL:KPP87448.1};
GN ORFNames=HLUCCO07_10400 {ECO:0000313|EMBL:KPP87448.1};
OS Rhodobacteraceae bacterium HLUCCO07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666914 {ECO:0000313|EMBL:KPP87448.1, ECO:0000313|Proteomes:UP000050369};
RN [1] {ECO:0000313|EMBL:KPP87448.1, ECO:0000313|Proteomes:UP000050369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO07 {ECO:0000313|EMBL:KPP87448.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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|ARBA:ARBA00001938};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPP87448.1}.
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DR EMBL; LJSU01000010; KPP87448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7VLS9; -.
DR STRING; 1666914.HLUCCO07_10400; -.
DR PATRIC; fig|1666914.4.peg.57; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000050369; 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; 2.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
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; 2.
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; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU361138}; Lipoyl {ECO:0000256|RuleBase:RU361138};
KW Transferase {ECO:0000256|RuleBase:RU361138, ECO:0000313|EMBL:KPP87448.1};
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 113..188
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 220..257
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 78..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 50731 MW; 8CCFAB6A9F9BA300 CRC64;
MATEVRVPTL GESVTEATVA TWFKQPGDSV AVDEMLCELE TDKVTVEVPS PAAGTLGEIV
AAEGDTVGVD ALLAMISESG EATPEKPKSE DKATKEDKPA KPAKAPAKSD GDTVDVMVPA
LGESVSEATV STWFKKVGDS VAQDEMLCEL ETDKVSVEVP APAAGVLVEI LAEEGSTVEA
SAKLARISGS ADGTVEPGPR PGAEEPKESG DDEDTGKDVE NAPSAEKMMA EAGLDPSQVK
GTGRDGRIMK EDVQKAIATG TSDARTSTPA PEPKPAASTP RAPVPADDAA REERVKMTRL
RQTIARRLKD AQNTAAILTT YNEVDMGAVM DLRNTYKDEF EKKHGVRLGF MSFFTKACVH
ALKEVPEVNA EIDGTDIVYK NFVHMGVAAG TPQGLVVPVI RDVDSKSFAQ IEKEIGEKGK
RARDGKLSMA EMQGGTFTLS NGGVYGSLMS CPRPSSTRRN RASSACTRSR TGPWSSKARS
//
