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 Q9ST62

Entry ID Method Resolution Chain Position Source
AF-Q9ST62-F1 Predicted AlphaFoldDB

No variants for Q9ST62

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9ST62

No associated diseases with Q9ST62

3 regional properties for Q9ST62

Type Name Position InterPro Accession
domain EF-hand domain 378 - 413 IPR002048
binding_site EF-Hand 1, calcium-binding site 391 - 403 IPR018247
domain FAD/NAD(P)-binding domain 56 - 381 IPR023753

Functions

Description
EC Number 1.6.5.9 With a quinone or similar compound as acceptor
Subcellular Localization
  • Mitochondrion inner membrane ; Peripheral membrane protein ; Intermembrane side
  • Peroxisome
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrial intermembrane space The region between the inner and outer lipid bilayers of the mitochondrial envelope.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

3 GO annotations of molecular function

Name Definition
calcium ion binding Binding to a calcium ion (Ca2+).
NADH dehydrogenase (quinone) activity Catalysis of the reaction: NADH + H+ + a quinone = NAD+ + a quinol.
oxidoreductase activity Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

1 GO annotations of biological process

Name Definition
NADH oxidation A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADH, to the oxidized form, NAD.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P32340 NDI1 Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q07500 NDE2 External NADH-ubiquinone oxidoreductase 2, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P40215 NDE1 External NADH-ubiquinone oxidoreductase 1, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
M1BYJ7 NDB1 External alternative NAD(P)H-ubiquinone oxidoreductase B1, mitochondrial Solanum tuberosum (Potato) PR
Q1JPL4 NDB1 External alternative NAD(P)H-ubiquinone oxidoreductase B1, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MRGFTYLSKV LHSHSSYSKL LVLCSVSTGG LLVYAESNVE SGKQVVEQNQ PESKKKRVVV
70 80 90 100 110 120
LGTGWGGTSF LKDVDISSYD VQVVSPRNYF AFTPLLPSVT CGTVEARSIV EPVRNIIKKR
130 140 150 160 170 180
SGEIQFWEAE CLKIDPVNRT VSCRSGINDN LAGHNDFSLQ YDYLVVAVGA QVNTFNTPGV
190 200 210 220 230 240
MEHCHFLKEV EDAQRIRRTV IDCFEKSVIP GLSEEERRTN LHFVIVGGGP TGVEFAAELH
250 260 270 280 290 300
DYVYEDLVKI YPSVKDFVKI TVIQSGDHIL NTFDERISSF AEQKFQRDGI EVSTGCRVTS
310 320 330 340 350 360
VSDHFINMKV KSTGKHVEVP YGMVVWSTGV GTRPFVKDFM EQVGQEKRRI LATDEWLRVK
370 380 390 400 410 420
GCSNVYALGD CASVDQHKVM EDISTIFEAA DKDDSGTLSV EEFRDVLEDI IIRYPQVDLY
430 440 450 460 470 480
LKNKHLLEAK DLFRDSEGNE REEVDIEGFK LALSHVDSQM KSLPATAQVA AQQGTYLARC
490 500 510 520 530 540
LNRWDQCKSN PEGPRRFKSS GRHEFLPFEY RHLGQFAPLG GDQAAAELPG DWVSMGHSTQ
550 560 570
WLWYSVYASK QVSWRTRYLV VGDWVRRYIF GRDSSRI