P36957 (ODO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
EC=2.3.1.61

Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2
Short name=OGDC-E2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
E2K

Gene names

Name:	DLST
Synonyms:	DLTS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic activity	Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently.
Pathway	Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
Subunit structure	Forms a 24-polypeptide structural core with octahedral symmetry.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Lipoyl Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-lysine catabolic process to acetyl-CoA via saccharopine Inferred from electronic annotation. Source: UniProtKB-UniPathway cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome lysine catabolic process Traceable author statement. Source: Reactome tricarboxylic acid cycle Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: HPA oxoglutarate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	dihydrolipoyllysine-residue succinyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 67	67	Mitochondrion Ref.8
	Chain	68 – 453	386	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial		PRO_0000020472
Regions
	Domain	71 – 143	73	Lipoyl-binding
Sites
	Active site	424	1	Potential
	Active site	428	1	Potential
Amino acid modifications
	Modified residue	110	1	N6-lipoyllysine Potential
Natural variations
	Natural variant	213	1	P → A. Ref.1 Ref.2 Corresponds to variant rs2853769 [ dbSNP | Ensembl ].		VAR_004976
	Natural variant	384	1	P → T.		VAR_004977
Experimental info
	Sequence conflict	14 – 15	2	RS → AP in BAA03871. Ref.1
	Sequence conflict	14 – 15	2	RS → AP in BAA05536. Ref.2
	Sequence conflict	14 – 15	2	RS → AP in AAB59629. Ref.3
	Sequence conflict	132	1	G → T in BAA03871. Ref.1
	Sequence conflict	212	1	E → D in BAA03871. Ref.1
	Sequence conflict	212	1	E → D in BAA05536. Ref.2
	Sequence conflict	312	1	R → T in BAA05536. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P36957 [UniParc]. Last modified January 11, 2011. Version 4. Checksum: A30E8CC959106B8F	FASTA	453	48,755
	10 20 30 40 50 60 MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPNSRKVVI NNSVFSVRFF 70 80 90 100 110 120 RTTAVCKDDL VTVKTPAFAE SVTEGDVRWE KAVGDTVAED EVVCEIETDK TSVQVPSPAN 130 140 150 160 170 180 GVIEALLVPD GGKVEGGTPL FTLRKTGAAP AKAKPAEAPA AAAPKAEPTA AAVPPPAAPI 190 200 210 220 230 240 PTQMPPVPSP SQPPSGKPVS AVKPTVAPPL AEPGAGKGLR SEHREKMNRM RQRIAQRLKE 250 260 270 280 290 300 AQNTCAMLTT FNEIDMSNIQ EMRARHKEAF LKKHNLKLGF MSAFVKASAF ALQEQPVVNA 310 320 330 340 350 360 VIDDTTKEVV YRDYIDISVA VATPRGLVVP VIRNVEAMNF ADIERTITEL GEKARKNELA 370 380 390 400 410 420 IEDMDGGTFT ISNGGVFGSL FGTPIINPPQ SAILGMHGIF DRPVAIGGKV EVRPMMYVAL 430 440 450 TYDHRLIDGR EAVTFLRKIK AAVEDPRVLL LDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3." Nakano K., Matsuda S., Sakamoto T., Takase C., Nakagawa S., Ohta S., Ariyama T., Inazawa J., Abe T., Miyata T. Biochim. Biophys. Acta 1216:360-368(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-213.
[2]	"Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex." Nakano K., Takase C., Sakamoto T., Nakagawa S., Inazawa J., Ohta S., Matuda S. Eur. J. Biochem. 224:179-189(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-213. Tissue: Peripheral blood.
[3]	"Physical mapping and nucleotide sequence analysis of the human dihydrolipoamide succinyltransferase gene." Keryanov S., Liang Y., Rogaev E.I., Sherrington R., Tsuda T., Rogaeva E., Chi H., Crapper-Mclachlan D., Chumakov Y., Rommens J.M., St George-Hyslop P.H. Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[8]	"Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini." Xu G., Shin S.B., Jaffrey S.R. Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 68-89. Tissue: Leukemic T-cell.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D16373 mRNA. Translation: BAA03871.1. D26535 Genomic DNA. Translation: BAA05536.1. L37418 mRNA. Translation: AAB59629.1. AK289414 mRNA. Translation: BAF82103.1. AC006530 Genomic DNA. Translation: AAD30181.1. CH471061 Genomic DNA. Translation: EAW81199.1. BC000302 mRNA. Translation: AAH00302.1. BC001922 mRNA. Translation: AAH01922.1.
IPI	IPI00420108.
PIR	PN0673. S39786.
RefSeq	NP_001924.2. NM_001933.4.
UniGene	Hs.525459.
3D structure databases
ProteinModelPortal	P36957.
SMR	P36957. Positions 73-140, 220-453.
ModBase	Search...
Protein-protein interaction databases
IntAct	P36957. 18 interactions.
MINT	MINT-3014449.
STRING	9606.ENSP00000335304.
PTM databases
PhosphoSite	P36957.
Polymorphism databases
DMDM	206729909.
2D gel databases
OGP	P36957.
UCD-2DPAGE	P36957.
Proteomic databases
PaxDb	P36957.
PRIDE	P36957.
Protocols and materials databases
DNASU	1743.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000334220; ENSP00000335304; ENSG00000119689.
GeneID	1743.
KEGG	hsa:1743.
UCSC	uc001xqs.3. human.
Organism-specific databases
CTD	1743.
GeneCards	GC14P075348.
H-InvDB	HIX0131240.
HGNC	HGNC:2911. DLST.
HPA	HPA003010.
MIM	126063. gene.
neXtProt	NX_P36957.
PharmGKB	PA27367.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281563.
HOVERGEN	HBG000268.
InParanoid	P36957.
KO	K00658.
OMA	IINMPQT.
OrthoDB	EOG4B2SZ1.
PhylomeDB	P36957.
Enzyme and pathway databases
BioCyc	MetaCyc:HS04324-MONOMER.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00868; UER00840.
Gene expression databases
ArrayExpress	P36957.
Bgee	P36957.
CleanEx	HS_DLST.
Genevestigator	P36957.
GermOnline	ENSG00000119689. Homo sapiens.
Family and domain databases
Gene3D	3.30.559.10. 1 hit.
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR023213. CAT-like_dom. IPR011053. Single_hybrid_motif. IPR006255. SucB. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. [Graphical view]
SUPFAM	SSF51230. Hybrid_motif. 1 hit.
TIGRFAMs	TIGR01347. sucB. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DLST. human.
GenomeRNAi	1743.
NextBio	7071.
SOURCE	Search...

Entry information

Entry name

ODO2_HUMAN

Accession

Primary (citable) accession number: P36957
Secondary accession number(s): Q7LDY7, Q9BQ32

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 149 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.