(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NPP5_YERPA

ID   A0A0E1NPP5_YERPA        Unreviewed;       407 AA.
AC   A0A0E1NPP5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   10-APR-2019, entry version 28.
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   OrderedLocusNames=YPA_0592 {ECO:0000313|EMBL:ABG12560.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12560.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12560.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12560.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG12560.1; -; Genomic_DNA.
DR   RefSeq; WP_002210727.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12560; ABG12560; YPA_0592.
DR   EnsemblBacteria; AJJ78875; AJJ78875; CH58_3450.
DR   KEGG; ypa:YPA_0592; -.
DR   PATRIC; fig|360102.15.peg.3618; -.
DR   KO; K00658; -.
DR   OMA; MKVPSPG; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000001971; Chromosome.
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; 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; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1NPP5.
DR   SWISS-2DPAGE; A0A0E1NPP5.
KW   Acyltransferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:ABG12560.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:ABG12560.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
SQ   SEQUENCE   407 AA;  44314 MW;  40AD12CC1E48F11B CRC64;
     MSSVDINVPD LPESVADGSV ATWHKKPGDS VKRDEVLVEI ETDKVILEVP ASQDGILDAI
     LEDEGATVTS RQVLGRIRPS DSSGKPTEEK SQSTESTPAQ RQTASLEEES NETLSPAIRR
     LIAEHDLDAT AIKGSGVGGR ITREDVDSHL ASRKSASAVV ADAKAVAAAA PVLAGRSEKR
     VPMSRLRKRV AERLLEAKNS TAMLTTFNEI NMQPIMDLRK QYGEAFEKRH GVRLGFMSFY
     IKAVVEALKR YPEVNASIDG EDVVYHNYFD VSIAVSTPRG LVTPVLRDVD TLSMADIEKK
     IKELAVKGRD GKLKVEELTG GNFTITNGGV FGSLMSTPII NPPQSAILGM HAIKDRPMAV
     NGQVVILPMM YLALSYDHRL IDGRESVGYL VTVKEMLEDP ARLLLDV
//

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