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Database: UniProt
Entry: A0A0H4UX79_9COXI
LinkDB: A0A0H4UX79_9COXI
Original site: A0A0H4UX79_9COXI 
ID   A0A0H4UX79_9COXI        Unreviewed;       405 AA.
AC   A0A0H4UX79;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   31-JUL-2019, entry version 21.
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   Name=sucB {ECO:0000313|EMBL:AKQ33355.1};
GN   ORFNames=CleRT_04010 {ECO:0000313|EMBL:AKQ33355.1};
OS   Coxiella-like endosymbiont.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae.
OX   NCBI_TaxID=1592897 {ECO:0000313|EMBL:AKQ33355.1};
RN   [1] {ECO:0000313|EMBL:AKQ33355.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRt {ECO:0000313|EMBL:AKQ33355.1};
RX   PubMed=26025560; DOI=10.1093/gbe/evv108;
RA   Gottlieb Y., Lalzar I., Klasson L.;
RT   "Distinctive Genome Reduction Rates Revealed by Genomic Analyses of
RT   Two Coxiella-Like Endosymbionts in Ticks.";
RL   Genome Biol. Evol. 7:1779-1796(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|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   -!- 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
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; CP011126; AKQ33355.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKQ33355; AKQ33355; CleRT_04010.
DR   KEGG; cey:CleRT_04010; -.
DR   PATRIC; fig|1592897.3.peg.802; -.
DR   KO; K00658; -.
DR   UniPathway; UPA00868; UER00840.
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; 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; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01347; sucB; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361138};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:AKQ33355.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        3     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      120    157       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       77    126       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     77    122       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   405 AA;  45716 MW;  AB5FE873800A8E29 CRC64;
     MPTIEIKVPM LPESVTDATV AKWYKKEGDS ISRDENLVDL ETDKVMLEVP APKDGIIKKI
     EVKEGRVVKA NEILAILEED HGEGEVEEEK KEKKDKDEDE VKKSEEEEKT KKKSEESESE
     LSPAVRRLVA EKGLDVNEIE GSGKEGRITK KDVEDYLEIQ KAKPAEKEIG KEEPTEKRVP
     LSRIRQRIAE RLVQVQQEAA LLTTFNEINM KSVMDLRKKY RDEFEKRHKV RLGLMSFFMK
     ASVEALKRFP MVNASIDGSE IIYHNYYDIG IAVGTERGLV VPVLRNAENM SMADIEKQIR
     EYGSRAQEGR LGIDELTGGT FTITNGGTYG SLLSTPIINP PQTAILGIHK IEDRPVVENG
     KIVIRPIMLV ALSYDHRVLD GREAVLFLVT IKELLEDPAR LVLGI
//
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