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Database: UniProt
Entry: A0A0E9M108_9BACT
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ID   A0A0E9M108_9BACT        Unreviewed;       396 AA.
AC   A0A0E9M108;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|ARBA:ARBA00019511};
DE            EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|ARBA:ARBA00032406};
DE   AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|ARBA:ARBA00030325};
GN   ORFNames=JCM15548_13585 {ECO:0000313|EMBL:GAO31238.1};
OS   Geofilum rubicundum JCM 15548.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC   Geofilum.
OX   NCBI_TaxID=1236989 {ECO:0000313|EMBL:GAO31238.1, ECO:0000313|Proteomes:UP000032900};
RN   [1] {ECO:0000313|EMBL:GAO31238.1, ECO:0000313|Proteomes:UP000032900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15548 {ECO:0000313|EMBL:GAO31238.1};
RX   PubMed=25736980;
RA   Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA   Hattori M., Ohkuma M.;
RT   "Distribution and evolution of nitrogen fixation genes in the phylum
RT   bacteroidetes.";
RL   Microbes Environ. 30:44-50(2015).
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).
CC       {ECO:0000256|ARBA:ARBA00004052}.
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:ARBA00001267};
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}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317}.
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:GAO31238.1}.
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DR   EMBL; BAZW01000041; GAO31238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E9M108; -.
DR   STRING; 1236989.JCM15548_13585; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000032900; Unassembled WGS sequence.
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   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
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   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032900};
KW   Transferase {ECO:0000313|EMBL:GAO31238.1};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          2..40
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00364"
FT   DOMAIN          156..382
FT                   /note="2-oxoacid dehydrogenase acyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00198"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          40..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..60
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  42904 MW;  81937EE8AAF9B3ED CRC64;
     MAEVESDKAT LSITAPESGK IQISVAAGST VKVNAIACKI DTSVEVPEEE EEDGAEDSEK
     EEVTDSQGKG TEKKAGAEQA AAEKSAKDKP ADKDTSSPLK TTPLARSKMA AEQLSADEVL
     KGLKKLSSRE VDTILDMRQN GDWSGSATQG TEASREQARK PMSNLRKQLS KRLVQVKNET
     AMLTTFNEVD MSALMDLRKK HQEAFVKKYG FKIGLISFFL KASAQALLHR PMVNSMLDGD
     DIITPNYVDI SVAMQSPKGL MVPVIRDVHS RSLAQIEEAM QTMATKVRSG KVSLEEMTGG
     TFTLTNGGVF GSMMSTPLIN PPQSAIIGMH NIVDRPVAIN GQVEIRPMMY IALSYDHRII
     DGKDSVGFLV DVKKAIENPV SLVFGGQNPE EMLLGL
//
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