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Database: UniProt
Entry: A0A1G9W0X5_9BACT
LinkDB: A0A1G9W0X5_9BACT
Original site: A0A1G9W0X5_9BACT 
ID   A0A1G9W0X5_9BACT        Unreviewed;       524 AA.
AC   A0A1G9W0X5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 10.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|RuleBase:RU361138};
DE            EC=2.3.1.61 {ECO:0000256|RuleBase:RU361138};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|RuleBase:RU361138};
GN   ORFNames=SAMN04488090_4205 {ECO:0000313|EMBL:SDM77841.1};
OS   Siphonobacter aquaeclarae.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Siphonobacter.
OX   NCBI_TaxID=563176 {ECO:0000313|EMBL:SDM77841.1, ECO:0000313|Proteomes:UP000198901};
RN   [1] {ECO:0000313|EMBL:SDM77841.1, ECO:0000313|Proteomes:UP000198901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21668 {ECO:0000313|EMBL:SDM77841.1,
RC   ECO:0000313|Proteomes:UP000198901};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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).
CC       {ECO:0000256|RuleBase:RU361138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate
CC         dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-
CC         (S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate
CC         dehydrogenase complex component E2] + CoA; Xref=Rhea:RHEA:15213,
CC         Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120;
CC         EC=2.3.1.61; Evidence={ECO:0000256|RuleBase:RU361138};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via
CC       saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
CC       {ECO:0000256|RuleBase:RU361138}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361138}.
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DR   EMBL; FNGS01000009; SDM77841.1; -; Genomic_DNA.
DR   BioCyc; GCF_900103285:BLR09_RS20985-MONOMER; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000198901; 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   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; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   TIGRFAMs; TIGR01347; sucB; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361138};
KW   Complete proteome {ECO:0000313|Proteomes:UP000198901};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198901};
KW   Transferase {ECO:0000256|RuleBase:RU361138};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        3     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      122    196       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      227    264       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION      265    298       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1G9W0X5}.
FT   COMPBIAS    268    284       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A1G9W0X5}.
SQ   SEQUENCE   524 AA;  54329 MW;  7011657D179580E3 CRC64;
     MAIIEMKVPV VGESVTEVTI ATWNKKEGDV VKMDEVLCEL ESDKATFELP AEASGTLHIL
     AKEGDTLPIG AVICSISTDG AAAPTNGVAA PAEAAPAPVA EPAAAPAAPV AEAPAASGET
     RVVEVKIPVM GESVTEATIA NWNKKEGDAV KMDEILCELE SDKATFELPA EVAGTLHIVA
     EPGATLPIGA VVATITVGTG AAVPASAPVA APAAAVASAV VADKAGAVTP VAAAILAEKG
     INPKDVQGSG EGGKVTKADA LKATTAPAPT PAPAPKPAAA PAPAAPAAPA GARAERRQRM
     TSLRKTIARR LVAVKNETAM LTTFNEVDMQ PIMELRSKFK DKFKEKHGVG LGFMSFFTKA
     VSVALKEFPA VNASIDGDEI VYHDYVDVSV AVSTERGLVV PILRNADQLS FAGIEKGILD
     LAVKARDNKL TIEDMSGGTF TITNGGVFGS MMSTPIINAP QVAILGMHNI VERPVVVNKE
     IVIRPMMYVA LSYDHRIIDG KESVSFLVRV KQLLEDPTRL LLDV
//
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