Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q28479

Entry ID Method Resolution Chain Position Source
AF-Q28479-F1 Predicted AlphaFoldDB

No variants for Q28479

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q28479

No associated diseases with Q28479

2 regional properties for Q28479

Type Name Position InterPro Accession
conserved_site Isocitrate/isopropylmalate dehydrogenase, conserved site 271 - 290 IPR019818
domain Isopropylmalate dehydrogenase-like domain 50 - 376 IPR024084

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mitochondrial isocitrate dehydrogenase complex (NAD+) Mitochondrial complex that possesses isocitrate dehydrogenase (NAD+) activity.

3 GO annotations of molecular function

Name Definition
magnesium ion binding Binding to a magnesium (Mg) ion.
NAD binding Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.

1 GO annotations of biological process

Name Definition
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
MAALSGVRWL TRALVSAGNP GAWRGLSTSA AAHAASRSQA EDVRVEGSFP VTMLPGDGVG
70 80 90 100 110 120
PELMHAVKEV FKAAAVPVEF QEHHLSEVQN MASEEKLEQV LSSMKENKVA IIGKIHTPME
130 140 150 160 170 180
YKGELASYDM RLRRKLDLFA NVVHVKSLPG YMTRHNNLDL VIIREQTEGE YSSLEHESAR
190 200 210 220 230 240
GVIECLKIVT RAKSQRIAKF AFDYATKKGR SKVTAVHKAN IMKLGDGLFL QCCEEVAELY
250 260 270 280 290 300
PKIKFETMII DNCCMQLVQN PYQFDVLVMP NLYGNIIDNL AAGLVGGAGV VPGESYSAEY
310 320 330 340 350 360
AVFETGARHP FAQAVGRNIA NPTAMLLSAS NMLRHLNLEY HSNMIADAVK KVIKVGKVRT
370 380
RDMGGYSTTT DFIKSVIGHL HPHGS