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Database: UniProt
Entry: ODO2_PSEAE
LinkDB: ODO2_PSEAE
Original site: ODO2_PSEAE 
ID   ODO2_PSEAE              Reviewed;         409 AA.
AC   Q9I3D2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAY-2019, entry version 112.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE            EC=2.3.1.61 {ECO:0000250|UniProtKB:P0AFG6};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2;
DE            Short=OGDC-E2;
DE   AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
GN   Name=sucB; OrderedLocusNames=PA1586;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
OS   JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
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:0000250|UniProtKB:P0AFG6}.
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:0000250|UniProtKB:P0AFG6};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via
CC       saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. Part of the 2-oxoglutarate dehydrogenase (OGDH) complex
CC       composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3).
CC       {ECO:0000250|UniProtKB:P0AFG6}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
DR   EMBL; AE004091; AAG04975.1; -; Genomic_DNA.
DR   PIR; H83448; H83448.
DR   RefSeq; NP_250277.1; NC_002516.2.
DR   RefSeq; WP_003114264.1; NZ_QZGE01000003.1.
DR   SMR; Q9I3D2; -.
DR   PaxDb; Q9I3D2; -.
DR   PRIDE; Q9I3D2; -.
DR   EnsemblBacteria; AAG04975; AAG04975; PA1586.
DR   GeneID; 881930; -.
DR   KEGG; pae:PA1586; -.
DR   PATRIC; fig|208964.12.peg.1645; -.
DR   PseudoCAP; PA1586; -.
DR   eggNOG; ENOG4105C7S; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281563; -.
DR   InParanoid; Q9I3D2; -.
DR   KO; K00658; -.
DR   OMA; MKVPSPG; -.
DR   PhylomeDB; Q9I3D2; -.
DR   BioCyc; PAER208964:G1FZ6-1616-MONOMER; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000002438; Chromosome.
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   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;
KW   Acyltransferase; Complete proteome; Lipoyl; Reference proteome;
KW   Transferase; Tricarboxylic acid cycle.
FT   CHAIN         1    409       Dihydrolipoyllysine-residue
FT                                succinyltransferase component of 2-
FT                                oxoglutarate dehydrogenase complex.
FT                                /FTId=PRO_0000287784.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   DOMAIN      112    149       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01170}.
FT   ACT_SITE    380    380       {ECO:0000250|UniProtKB:P0AFG6}.
FT   ACT_SITE    384    384       {ECO:0000250|UniProtKB:P0AFG6}.
FT   MOD_RES      43     43       N6-lipoyllysine. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
SQ   SEQUENCE   409 AA;  42887 MW;  01FCCEB71E04353C CRC64;
     MAIEIKAPTF PESVADGTVA TWHKKPGEAV KRDELIVDIE TDKVVIEVLA EADGVLAEII
     KNEGDTVLSN ELLGKLNEGG AAAPAAPAAA APAAAPAAQA AAPAAAGGDD AILSPAARKL
     AEEAGIDPNS IAGTGKGGRV TKEDVVAAVE AKKNAPAAPA KPAAPAAEAP IFAAGDRVEK
     RVPMTRLRAK VAERLVEAQS AMAMLTTFNE VNMKPIMDLR SKYKDLFEKK HNGVRLGFMS
     FFVKAATEAL KRFPGVNASI DGNDIVYHGY QDIGVAVSSD RGLVVPVLRN AEFMSLAEIE
     GGIANFGKKA KEGKLTIEDM TGGTFTISNG GVFGSLLSTP IVNPPQTAIL GMHKIQERPM
     AVNGQVVILP MMYLALSYDH RLIDGKEAVS FLVAIKDLLE DPARLLLDV
//
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