Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P11179

- ODO2_BOVIN

UniProt

P11179 - ODO2_BOVIN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

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

Gene

DLST

Organism
Bos taurus (Bovine)
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).

Catalytic activityi

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

Cofactori

Binds 1 lipoyl cofactor covalently.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei426 – 4261Sequence Analysis
Active sitei430 – 4301Sequence Analysis

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

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
Gene namesi
Name:DLST
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
  2. oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6868MitochondrionBy similarityAdd
BLAST
Chaini69 – 455387Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000162252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111N6-lipoyllysine1 Publication
Modified residuei155 – 1551N6-acetyllysineBy similarity
Modified residuei269 – 2691N6-acetyllysineBy similarity
Modified residuei274 – 2741N6-acetyllysineBy similarity
Modified residuei275 – 2751N6-acetyllysineBy similarity
Modified residuei279 – 2791N6-acetyllysineBy similarity
Modified residuei309 – 3091N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP11179.
PRIDEiP11179.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

IntActiP11179. 1 interaction.
STRINGi9913.ENSBTAP00000052502.

Structurei

3D structure databases

ProteinModelPortaliP11179.
SMRiP11179. Positions 226-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.Curated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
HOVERGENiHBG000268.
InParanoidiP11179.
KOiK00658.

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.

P11179-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSRSRCASR AFSRSLSAFQ KGNCPLVRRS LPGISLCQGP GYPDSRKTVI
60 70 80 90 100
NSSNIFSVRF FRTTAVCKDD VITVKTPAFA ESVTEGDVRW EKAVGDTVAE
110 120 130 140 150
DEVVCEIETD KTSVQVPSPA NGVIEALLVP DGGKVEGGTP LFTLRKTGAA
160 170 180 190 200
PAKAKPAAAP AAAAPKAEPT VSAVPPPPAA PIPTQMPPVP SPSQPLTSKP
210 220 230 240 250
VSAVKPTAAP PRAEAGAGVG LRSEHREKMN RMRQRIAQRL KEAQNTCAML
260 270 280 290 300
TTFNEIDMSN IQEMRARHKD AFLKKHNLKL GFMSAFVKAS AFALQEQPVV
310 320 330 340 350
NAVIDDATKE VVYRDYIDIS VAVATPRGLV VPVIRNVETM NYADIERTIS
360 370 380 390 400
ELGEKARKNE LAIEDMDGGT FTISNGGVFG SLFGTPIINP PQSAILGMHA
410 420 430 440 450
IVDRPVVIGG KVEVRPMMYV ALTYDHRLID GREAVTFLRK IKAAVEDPRV

LLLDL
Length:455
Mass (Da):48,973
Last modified:October 17, 2006 - v2
Checksum:iDB2124A4D06C389B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BT026207 mRNA. Translation: ABG67046.1.
PIRiS00123.
RefSeqiNP_001068750.1. NM_001075282.1.
UniGeneiBt.41191.

Genome annotation databases

GeneIDi506888.
KEGGibta:506888.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BT026207 mRNA. Translation: ABG67046.1 .
PIRi S00123.
RefSeqi NP_001068750.1. NM_001075282.1.
UniGenei Bt.41191.

3D structure databases

ProteinModelPortali P11179.
SMRi P11179. Positions 226-452.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P11179. 1 interaction.
STRINGi 9913.ENSBTAP00000052502.

Proteomic databases

PaxDbi P11179.
PRIDEi P11179.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 506888.
KEGGi bta:506888.

Organism-specific databases

CTDi 1743.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281563.
HOVERGENi HBG000268.
InParanoidi P11179.
KOi K00658.

Enzyme and pathway databases

UniPathwayi UPA00868 ; UER00840 .

Miscellaneous databases

NextBioi 20867785.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "Amino acid sequence surrounding the lipoic acid cofactor of bovine kidney 2-oxoglutarate dehydrogenase complex."
    Bradford A.P., Aitken A., Beg F., Cook K.G., Yeaman S.J.
    FEBS Lett. 222:211-214(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 107-122, LIPOYLATION AT LYS-111.
    Tissue: Kidney.

Entry informationi

Entry nameiODO2_BOVIN
AccessioniPrimary (citable) accession number: P11179
Secondary accession number(s): Q0V8L1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 103 of the entry and version 2 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