(data stored in SCRATCH zone)

SWISSPROT: A1AZH2_PARDP

ID   A1AZH2_PARDP            Unreviewed;       510 AA.
AC   A1AZH2;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 92.
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=Pden_0554 {ECO:0000313|EMBL:ABL68666.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68666.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000489; ABL68666.1; -; Genomic_DNA.
DR   RefSeq; WP_011746899.1; NC_008686.1.
DR   STRING; 318586.Pden_0554; -.
DR   PRIDE; A1AZH2; -.
DR   EnsemblBacteria; ABL68666; ABL68666; Pden_0554.
DR   KEGG; pde:Pden_0554; -.
DR   eggNOG; ENOG4105C7S; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281563; -.
DR   KO; K00658; -.
DR   OMA; MKVPSPG; -.
DR   BioCyc; PDEN318586:G1GW1-557-MONOMER; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000000361; Chromosome 1.
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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AZH2.
DR   SWISS-2DPAGE; A1AZH2.
KW   Acyltransferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:ABL68666.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:ABL68666.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      108    183       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      216    253       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   510 AA;  53904 MW;  4C55F19D3DE158C6 CRC64;
     MAVELRVPTL GESVSEATVA TWFKKPGDRV AVDEMLCELE TDKVTVEVPS PVAGKLAEIV
     APEGAVVAPN ALLAQIMEQG DAGPEEMLPK ADAGTKAQEG QRNMSGKSVD VMVPTLGESV
     TEATVATWFK KVGDSVAQDE MLCELETDKV SVEVPAPAAG VLAEILAPEG ATVDASAKLA
     IITEGAAGVA KAEAPAAAVQ SPGAGPETPA PRKDVEDAPS AKKAMAEAGV SRDAVTGTGR
     DGRVMKEDVA RAASAPQAAS PAPAPAQAPR APSSADDAAR EERVKMTRLR ATIARRLKDA
     QNTAAMLTTY NEVDMKGIMD LRNTYKDQFE KKHKVKLGFM SFFVKACCHA LKEVPEVNAE
     IDGGDVVYKN FVHMGVAVGT PNGLVVPVVR DADQKSFARI EKEIAELGTR ARDGKLTMAE
     MQGGTFTISN GGVYGSLMSS PILNPPQSGI LGMHKIQDRP VVVDGQIVIR PMMYLALSYD
     HRIVDGKGAV TFLVRVKEAL EDPRRLLMDL
//

If you have problems or comments...

PBIL Back to PBIL home page