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Q9N0F1

- ODO2_PIG

UniProt

Q9N0F1 - ODO2_PIG

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Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial

Gene
DLST
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

Cofactori

Binds 1 lipoyl cofactor covalently By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei426 – 4261 Reviewed prediction
Active sitei430 – 4301 Reviewed prediction

GO - Molecular functioni

  1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  2. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiREACT_205223. Lysine catabolism.
REACT_217226. Citric acid cycle (TCA cycle).
UniPathwayiUPA00868; UER00840.

Names & Taxonomyi

Protein namesi
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
E2o
Short name:
PE2o
Gene namesi
Name:DLST
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Chromosome 7

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
  2. nucleus Source: Ensembl
  3. oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi374 – 3741S → A: Loss of activity.
Mutagenesisi426 – 4261H → C: 16% of activity.
Mutagenesisi430 – 4301D → A, E or N: Loss of activity.
Mutagenesisi451 – 4533LLL → AAA or DDD: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6868MitochondrionAdd
BLAST
Chaini69 – 455387Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020474Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111N6-lipoyllysine Reviewed prediction
Modified residuei155 – 1551N6-acetyllysine By similarity
Modified residuei269 – 2691N6-acetyllysine By similarity
Modified residuei274 – 2741N6-acetyllysine By similarity
Modified residuei275 – 2751N6-acetyllysine By similarity
Modified residuei279 – 2791N6-acetyllysine By similarity
Modified residuei309 – 3091N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9N0F1.
PRIDEiQ9N0F1.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9N0F1.
SMRiQ9N0F1. Positions 222-455.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 14473Lipoyl-bindingAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni221 – 453233CatalyticAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi151 – 21565Pro-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
GeneTreeiENSGT00740000115255.
HOGENOMiHOG000281563.
HOVERGENiHBG000268.
KOiK00658.
OMAiAEDEVIC.
OrthoDBiEOG78PV93.
TreeFamiTF314164.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9N0F1-1 [UniParc]FASTAAdd to Basket

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MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGISLCQGP GYPDSRKIVI    50
SNSSVLNVRF FRTTAVCKDD VITVKTPAFA ESVTEGDVRW EKAVGDTVAE 100
DEVVCEIETD KTSVQVPSPA NGVIEALLVP DGGKVEGGTP LFTLRKTGAA 150
PAKAKPAEAP AAAAPKAEPA VSAVPPPPAA SIPTQMPPVP SPPQPLTSKP 200
VSAVKPTAAP PVAEPGAVKG LRAEHREKMN RMRQRIAQRL KEAQNTCAML 250
TTFNEIDMSN IQDMRARHKE AFLKKHNLKL GFMSAFVKAS AFALQEQPVV 300
NAVIDDTTKE VVYRDYIDIS VAVATPRGLV VPVIRNVETM NYADIERTIS 350
ELGEKARKNE LAIEDMDGGT FTISNGGVFG SLFGTPIINP PQSAILGMHA 400
IVDRPVAVGG KVEIRPMMYV ALTYDHRLID GREAVTFLRK IKAAVEDPRV 450
LLLDL 455
Length:455
Mass (Da):48,977
Last modified:October 1, 2000 - v1
Checksum:i563B5E7455C842FA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB035206 mRNA. Translation: BAA95700.1.
RefSeqiNP_999562.1. NM_214397.1.
UniGeneiSsc.2730.

Genome annotation databases

EnsembliENSSSCT00000002639; ENSSSCP00000002572; ENSSSCG00000002374.
GeneIDi397690.
KEGGissc:397690.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB035206 mRNA. Translation: BAA95700.1 .
RefSeqi NP_999562.1. NM_214397.1.
UniGenei Ssc.2730.

3D structure databases

ProteinModelPortali Q9N0F1.
SMRi Q9N0F1. Positions 222-455.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q9N0F1.
PRIDEi Q9N0F1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000002639 ; ENSSSCP00000002572 ; ENSSSCG00000002374 .
GeneIDi 397690.
KEGGi ssc:397690.

Organism-specific databases

CTDi 1743.

Phylogenomic databases

eggNOGi COG0508.
GeneTreei ENSGT00740000115255.
HOGENOMi HOG000281563.
HOVERGENi HBG000268.
KOi K00658.
OMAi AEDEVIC.
OrthoDBi EOG78PV93.
TreeFami TF314164.

Enzyme and pathway databases

UniPathwayi UPA00868 ; UER00840 .
Reactomei REACT_205223. Lysine catabolism.
REACT_217226. Citric acid cycle (TCA cycle).

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
InterProi 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 ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view ]
SUPFAMi SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01347. sucB. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, overexpression and mutagenesis of cDNA encoding dihydrolipoamide succinyltransferase component of the porcine 2-oxoglutarate dehydrogenase complex."
    Koike K., Suematsu T., Ehara M.
    Eur. J. Biochem. 267:3005-3016(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS.
    Tissue: Brain cortex and Heart.

Entry informationi

Entry nameiODO2_PIG
AccessioniPrimary (citable) accession number: Q9N0F1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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