P19262

PR
Gene name
KGD2 (YDR148C, YD8358.05C)
Protein name
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Names
2-oxoglutarate dehydrogenase complex component E2, OGDC-E2, Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YDR148C
EC number
2.3.1.61: Transferring groups other than amino-acyl groups
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

127-254 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P19262

Entry ID Method Resolution Chain Position Source
AF-P19262-F1 Predicted AlphaFoldDB

1 variants for P19262

Variant ID(s) Position Change Description Diseaes Association Provenance
s04-754561 168 A>V No SGRP

No associated diseases with P19262

3 regional properties for P19262

Type Name Position InterPro Accession
domain Biotin/lipoyl attachment 73 - 148 IPR000089
domain 2-oxoacid dehydrogenase acyltransferase, catalytic domain 233 - 462 IPR001078
binding_site 2-oxo acid dehydrogenase, lipoyl-binding site 98 - 127 IPR003016

Functions

Description
EC Number 2.3.1.61 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
mitochondrial alpha-ketoglutarate dehydrogenase complex Mitochondrial complex that possesses alpha-ketoglutarate dehydrogenase activity.
mitochondrial nucleoid The region of a mitochondrion to which the DNA is confined.
mitochondrial oxoglutarate dehydrogenase complex A complex of multiple copies of three enzymatic components: oxoglutarate dehydrogenase (lipoamide) (E1), dihydrolipoamide S-succinyltransferase (E2) and dihydrolipoamide dehydrogenase (E3); catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and carbon dioxide (CO2) within the mitochondrial matrix. An example of this complex is found in Mus musculus.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

1 GO annotations of molecular function

Name Definition
dihydrolipoyllysine-residue succinyltransferase activity Catalysis of the reaction: succinyl-CoA + dihydrolipoamide = CoA + S-succinyldihydrolipoamide.

3 GO annotations of biological process

Name Definition
2-oxoglutarate metabolic process The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
L-lysine catabolic process to acetyl-CoA via saccharopine The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including acetyl-CoA, via the intermediate saccharopine.
tricarboxylic acid cycle A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLSRATRTAA AKSLVKSKVA RNVMAASFVK RHASTSLFKQ ANKVESLGSI YLSGKKISVA
70 80 90 100 110 120
ANPFSITSNR FKSTSIEVPP MAESLTEGSL KEYTKNVGDF IKEDELLATI ETDKIDIEVN
130 140 150 160 170 180
SPVSGTVTKL NFKPEDTVTV GEELAQVEPG EAPAEGSGES KPEPTEQAEP SQGVAARENS
190 200 210 220 230 240
SEETASKKEA APKKEAAPKK EVTEPKKADQ PKKTVSKAQE PPVASNSFTP FPRTETRVKM
250 260 270 280 290 300
NRMRLRIAER LKESQNTAAS LTTFNEVDMS ALMEMRKLYK DEIIKKTGTK FGFMGLFSKA
310 320 330 340 350 360
CTLAAKDIPA VNGAIEGDQI VYRDYTDISV AVATPKGLVT PVVRNAESLS VLDIENEIVR
370 380 390 400 410 420
LSHKARDGKL TLEDMTGGTF TISNGGVFGS LYGTPIINSP QTAVLGLHGV KERPVTVNGQ
430 440 450 460
IVSRPMMYLA LTYDHRLLDG REAVTFLKTV KELIEDPRKM LLW