ID ODO2_RAT Reviewed; 454 AA.
AC Q01205; Q5XI35;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-APR-2013, entry version 119.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial;
DE EC=2.3.1.61;
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2;
DE Short=OGDC-E2;
DE AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE AltName: Full=E2K;
DE Flags: Precursor;
GN Name=Dlst;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-454, AND PROTEIN SEQUENCE OF 69-83.
RC TISSUE=Heart;
RX PubMed=1918017;
RA Nakano K., Matuda S., Yamanaka T., Tsubouchi H., Nakagawa S.,
RA Titani K., Ohta S., Miyata T.;
RT "Purification and molecular cloning of succinyltransferase of the rat
RT alpha-ketoglutarate dehydrogenase complex. Absence of a sequence motif
RT of the putative E3 and/or E1 binding site.";
RL J. Biol. Chem. 266:19013-19017(1991).
RN [3]
RP PROTEIN SEQUENCE OF 69-89; 135-145; 262-308 AND 314-326, AND MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Chen W.-Q., Afjehi-Sadat L., Diao W.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC contains multiple copies of 3 enzymatic components: 2-oxoglutarate
CC dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC lipoamide dehydrogenase (E3).
CC -!- CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N(6)-
CC (dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-
CC succinyldihydrolipoyl)lysine.
CC -!- COFACTOR: Binds 1 lipoyl cofactor covalently.
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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC -!- SIMILARITY: Contains 1 lipoyl-binding domain.
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DR EMBL; BC083858; AAH83858.1; -; mRNA.
DR EMBL; D90401; BAA14397.1; -; mRNA.
DR IPI; IPI00551702; -.
DR PIR; A41015; A41015.
DR RefSeq; NP_001006982.2; NM_001006981.2.
DR UniGene; Rn.99702; -.
DR ProteinModelPortal; Q01205; -.
DR SMR; Q01205; 221-454.
DR IntAct; Q01205; 1.
DR PhosphoSite; Q01205; -.
DR PaxDb; Q01205; -.
DR PRIDE; Q01205; -.
DR GeneID; 299201; -.
DR KEGG; rno:299201; -.
DR UCSC; RGD:1359615; rat.
DR CTD; 1743; -.
DR RGD; 1359615; Dlst.
DR eggNOG; COG0508; -.
DR HOGENOM; HOG000281563; -.
DR HOVERGEN; HBG000268; -.
DR InParanoid; Q01205; -.
DR KO; K00658; -.
DR OrthoDB; EOG4B2SZ1; -.
DR BRENDA; 2.3.1.61; 5301.
DR UniPathway; UPA00868; UER00840.
DR NextBio; 644993; -.
DR ArrayExpress; Q01205; -.
DR Genevestigator; Q01205; -.
DR GermOnline; ENSRNOG00000005061; Rattus norvegicus.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IDA:RGD.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:RGD.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0006734; P:NADH metabolic process; IDA:RGD.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IC:RGD.
DR Gene3D; 3.30.559.10; -; 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.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR006255; SucB.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF51230; Hybrid_motif; 1.
DR TIGRFAMs; TIGR01347; sucB; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Complete proteome; Direct protein sequencing; Lipoyl;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1 68 Mitochondrion.
FT CHAIN 69 454 Dihydrolipoyllysine-residue
FT succinyltransferase component of 2-
FT oxoglutarate dehydrogenase complex,
FT mitochondrial.
FT /FTId=PRO_0000020475.
FT DOMAIN 72 144 Lipoyl-binding.
FT ACT_SITE 425 425 Potential.
FT ACT_SITE 429 429 Potential.
FT MOD_RES 111 111 N6-lipoyllysine (Potential).
FT CONFLICT 13 13 S -> M (in Ref. 2; BAA14397).
FT CONFLICT 52 54 NSS -> TVA (in Ref. 2; BAA14397).
FT CONFLICT 164 164 Y -> H (in Ref. 2; BAA14397).
FT CONFLICT 281 281 F -> L (in Ref. 2; BAA14397).
FT CONFLICT 448 448 R -> A (in Ref. 2; BAA14397).
SQ SEQUENCE 454 AA; 48925 MW; 2818F530F4B7C683 CRC64;
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPDSRKMVI NNSSVFSVRF
FQTTAVCKND VITVQTPAFA ESVTEGDVRW EKAVGDAVAE DEVVCEIETD KTSVQVPSPA
NGIIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAEAP ATAYKAAPEA PAAPPPPVAP
VPTQMPPVPS PSQPPSSKPV SAIKPTAAPP LAEAGAAKGL RSEHREKMNR MRQRIAQRLK
EAQNTCAMLT TFNEVDMSNI QEMRARHKDA FLKKHNLKLG FMSAFVKASA FALQEQPVVN
AVIDDATKEV VYRDYIDISV AVATPRGLVV PVIRNVETMN YADIERTINE LGEKARKNEL
AIEDMDGGTF TISNGGVFGS LFGTPIINPP QSAILGMHGI FDRPVAVGGK VEVRPMMYVA
LTYDHRLIDG REAVTFLRKI KAAVEDPRVL LLDL
//
