ID ODO2_HUMAN Reviewed; 453 AA.
AC P36957; Q7LDY7; Q9BQ32;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 01-MAY-2013, entry version 149.
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; Synonyms=DLTS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-213.
RX PubMed=8268217; DOI=10.1016/0167-4781(93)90002-U;
RA Nakano K., Matsuda S., Sakamoto T., Takase C., Nakagawa S., Ohta S.,
RA Ariyama T., Inazawa J., Abe T., Miyata T.;
RT "Human dihydrolipoamide succinyltransferase: cDNA cloning and
RT localization on chromosome 14q24.2-q24.3.";
RL Biochim. Biophys. Acta 1216:360-368(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-213.
RC TISSUE=Peripheral blood;
RX PubMed=8076640; DOI=10.1111/j.1432-1033.1994.tb20010.x;
RA Nakano K., Takase C., Sakamoto T., Nakagawa S., Inazawa J., Ohta S.,
RA Matuda S.;
RT "Isolation, characterization and structural organization of the gene
RT and pseudogene for the dihydrolipoamide succinyltransferase component
RT of the human 2-oxoglutarate dehydrogenase complex.";
RL Eur. J. Biochem. 224:179-189(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RA Keryanov S., Liang Y., Rogaev E.I., Sherrington R., Tsuda T.,
RA Rogaeva E., Chi H., Crapper-Mclachlan D., Chumakov Y., Rommens J.M.,
RA St George-Hyslop P.H.;
RT "Physical mapping and nucleotide sequence analysis of the human
RT dihydrolipoamide succinyltransferase gene.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 68-89.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective
RT labeling of protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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; D16373; BAA03871.1; -; mRNA.
DR EMBL; D26535; BAA05536.1; -; Genomic_DNA.
DR EMBL; L37418; AAB59629.1; -; mRNA.
DR EMBL; AK289414; BAF82103.1; -; mRNA.
DR EMBL; AC006530; AAD30181.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81199.1; -; Genomic_DNA.
DR EMBL; BC000302; AAH00302.1; -; mRNA.
DR EMBL; BC001922; AAH01922.1; -; mRNA.
DR IPI; IPI00420108; -.
DR PIR; S39786; PN0673.
DR RefSeq; NP_001924.2; NM_001933.4.
DR UniGene; Hs.525459; -.
DR ProteinModelPortal; P36957; -.
DR SMR; P36957; 73-140, 220-453.
DR IntAct; P36957; 18.
DR MINT; MINT-3014449; -.
DR STRING; 9606.ENSP00000335304; -.
DR PhosphoSite; P36957; -.
DR DMDM; 206729909; -.
DR OGP; P36957; -.
DR UCD-2DPAGE; P36957; -.
DR PaxDb; P36957; -.
DR PRIDE; P36957; -.
DR DNASU; 1743; -.
DR Ensembl; ENST00000334220; ENSP00000335304; ENSG00000119689.
DR GeneID; 1743; -.
DR KEGG; hsa:1743; -.
DR UCSC; uc001xqs.3; human.
DR CTD; 1743; -.
DR GeneCards; GC14P075348; -.
DR H-InvDB; HIX0131240; -.
DR HGNC; HGNC:2911; DLST.
DR HPA; HPA003010; -.
DR MIM; 126063; gene.
DR neXtProt; NX_P36957; -.
DR PharmGKB; PA27367; -.
DR eggNOG; COG0508; -.
DR HOGENOM; HOG000281563; -.
DR HOVERGEN; HBG000268; -.
DR InParanoid; P36957; -.
DR KO; K00658; -.
DR OMA; IINMPQT; -.
DR OrthoDB; EOG4B2SZ1; -.
DR PhylomeDB; P36957; -.
DR BioCyc; MetaCyc:HS04324-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00868; UER00840.
DR ChiTaRS; DLST; human.
DR GenomeRNAi; 1743; -.
DR NextBio; 7071; -.
DR ArrayExpress; P36957; -.
DR Bgee; P36957; -.
DR CleanEx; HS_DLST; -.
DR Genevestigator; P36957; -.
DR GermOnline; ENSG00000119689; Homo sapiens.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:EC.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0006554; P:lysine catabolic process; TAS:Reactome.
DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome.
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; Polymorphism; Reference proteome; Transferase;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1 67 Mitochondrion.
FT CHAIN 68 453 Dihydrolipoyllysine-residue
FT succinyltransferase component of 2-
FT oxoglutarate dehydrogenase complex,
FT mitochondrial.
FT /FTId=PRO_0000020472.
FT DOMAIN 71 143 Lipoyl-binding.
FT ACT_SITE 424 424 Potential.
FT ACT_SITE 428 428 Potential.
FT MOD_RES 110 110 N6-lipoyllysine (Potential).
FT VARIANT 213 213 P -> A (in dbSNP:rs2853769).
FT /FTId=VAR_004976.
FT VARIANT 384 384 P -> T.
FT /FTId=VAR_004977.
FT CONFLICT 14 15 RS -> AP (in Ref. 1; BAA03871, 2;
FT BAA05536 and 3; AAB59629).
FT CONFLICT 132 132 G -> T (in Ref. 1; BAA03871).
FT CONFLICT 212 212 E -> D (in Ref. 1; BAA03871 and 2;
FT BAA05536).
FT CONFLICT 312 312 R -> T (in Ref. 2; BAA05536).
SQ SEQUENCE 453 AA; 48755 MW; A30E8CC959106B8F CRC64;
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPNSRKVVI NNSVFSVRFF
RTTAVCKDDL VTVKTPAFAE SVTEGDVRWE KAVGDTVAED EVVCEIETDK TSVQVPSPAN
GVIEALLVPD GGKVEGGTPL FTLRKTGAAP AKAKPAEAPA AAAPKAEPTA AAVPPPAAPI
PTQMPPVPSP SQPPSGKPVS AVKPTVAPPL AEPGAGKGLR SEHREKMNRM RQRIAQRLKE
AQNTCAMLTT FNEIDMSNIQ EMRARHKEAF LKKHNLKLGF MSAFVKASAF ALQEQPVVNA
VIDDTTKEVV YRDYIDISVA VATPRGLVVP VIRNVEAMNF ADIERTITEL GEKARKNELA
IEDMDGGTFT ISNGGVFGSL FGTPIINPPQ SAILGMHGIF DRPVAIGGKV EVRPMMYVAL
TYDHRLIDGR EAVTFLRKIK AAVEDPRVLL LDL
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