Reviewed, UniProtKB/Swiss-Prot Q90512 (ODO2_FUGRU)

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

Gene names

Name:

dlst

Organism

Fugu rubripes (Japanese pufferfish) (Takifugu rubripes)

Taxonomic identifier

31033 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Tetraodontiformes › Tetradontoidea › Tetraodontidae › Takifugu

Protein attributes

Sequence length	409 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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 three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently By similarity.
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 By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Lipoyl Transit peptide
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell oxoglutarate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	dihydrolipoyllysine-residue succinyltransferase activity Inferred from electronic annotation. Source: EC lipoic acid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	‹1 – 36	›36	Mitochondrion By similarity
	Chain	37 – 409	373	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial		PRO_0000020476
Regions
	Domain	40 – 112	73	Lipoyl-binding
	Compositional bias	133 – 139	7	Poly-Pro
Sites
	Active site	380	1	Potential
	Active site	384	1	Potential
Amino acid modifications
	Modified residue	79	1	N6-lipoyllysine Potential
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q90512-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5A429FD99DA43873	FASTA	409	44,112
	10 20 30 40 50 60 SSVCRRLIFR TSRPGERASS QNSFHVRYFR TSVVHRDDLV TVKTPAFAES VTEGDVRWEK 70 80 90 100 110 120 AVGDSVTEDE VVCEIETDKT SVQVPSPAAG VIEELLVPDG GKVEGGTPLF KLRKGAAAEA 130 140 150 160 170 180 APSSVTEPVT AAPPPPPPPV SAPTAMPSVP PVPTQALQAK PVPAPTLPEP STLGGRGESR 190 200 210 220 230 240 VKMSRMRLRI AQRLKEAQNT CAMLTTFNEV DMSNIQEMRT LHKDAFLKKH SIKLGFMSAF 250 260 270 280 290 300 VKAAAHALTD QPAVNAVIDG ATNEIVYRDY VDISVAVATP KGLVVPVIRN VETMNFADIE 310 320 330 340 350 360 RTINALGEKA RNNELAVEDM DGGTFTISNG GVFGSLFGTP IINPPQSAIL GMHGIFQRPV 370 380 390 400 AVDGKAEIRP MMYVALTYDH RLVDGREAVT FLRKIKAAVE DPRALLLDM

References

[1]

"Conservation of synteny between the genome of the pufferfish (Fugu rubripes) and the region on human chromosome 14 (14q24.3) associated with familial Alzheimer disease (AD3 locus)." Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J., Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R., Rogaev E.I., St George-Hyslop P.H., Brenner S., Dykes C.W. Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996) [PubMed: 8643637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	U40758 Genomic DNA. Translation: AAC59779.1.
3D structure databases
HSSP	HSSP built from PDB template 1C4T based on UniProtKB P07016.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q90512.
Enzyme and pathway databases
BRENDA	2.3.1.61. 281122.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR006255. SucB. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. [Graphical view]
ProDom	PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01347. sucB. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODO2_FUGRU

Accession

Primary (citable) accession number: Q90512

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)