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

10 structures for P32340

Entry ID Method Resolution Chain Position Source
4G6G X-ray 239 A A/B 24-513 PDB
4G6H X-ray 226 A A/B 24-513 PDB
4G73 X-ray 252 A A/B 24-513 PDB
4G74 X-ray 248 A A/B 24-513 PDB
4G9K X-ray 270 A A/B 43-513 PDB
4GAP X-ray 290 A A/B 43-513 PDB
4GAV X-ray 300 A A/B 43-513 PDB
5YJW X-ray 185 A A 30-513 PDB
5YJX X-ray 321 A A/B 28-513 PDB
AF-P32340-F1 Predicted AlphaFoldDB

6 variants for P32340

Variant ID(s) Position Change Description Diseaes Association Provenance
s13-29779 10 K>R No SGRP
s13-29765 15 S>T No SGRP
s13-29750 20 V>I No SGRP
s13-29401 136 R>K No SGRP
s13-28715 365 A>T No SGRP
s13-28519 430 L>W No SGRP

No associated diseases with P32340

1 regional properties for P32340

Type Name Position InterPro Accession
domain FAD/NAD(P)-binding domain 55 - 400 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 ; Matrix side
  • Bound to the mitochondrial inner membrane facing the matrix site
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 matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
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.

2 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
NADH dehydrogenase (ubiquinone) activity Catalysis of the reaction: NADH + ubiquinone + 5 H(+)(in) <=> NAD(+) + ubiquinol + 4 H(+)(out).

3 GO annotations of biological process

Name Definition
mitochondrial electron transport, NADH to ubiquinone The transfer of electrons from NADH to ubiquinone that occurs during oxidative phosphorylation.
NADH oxidation A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADH, to the oxidized form, NAD.
positive regulation of apoptotic process Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
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
Q9ST62 NDB1 External alternative NAD(P)H-ubiquinone oxidoreductase B1, mitochondrial Solanum tuberosum (Potato) PR
F4JJJ3 NDB3 External alternative NAD(P)H-ubiquinone oxidoreductase B3, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
Q94BV7 NDB2 External alternative NAD(P)H-ubiquinone oxidoreductase B2, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
Q1JPL4 NDB1 External alternative NAD(P)H-ubiquinone oxidoreductase B1, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MLSKNLYSNK RLLTSTNTLV RFASTRSTGV ENSGAGPTSF KTMKVIDPQH SDKPNVLILG
70 80 90 100 110 120
SGWGAISFLK HIDTKKYNVS IISPRSYFLF TPLLPSAPVG TVDEKSIIEP IVNFALKKKG
130 140 150 160 170 180
NVTYYEAEAT SINPDRNTVT IKSLSAVSQL YQPENHLGLH QAEPAEIKYD YLISAVGAEP
190 200 210 220 230 240
NTFGIPGVTD YGHFLKEIPN SLEIRRTFAA NLEKANLLPK GDPERRRLLS IVVVGGGPTG
250 260 270 280 290 300
VEAAGELQDY VHQDLRKFLP ALAEEVQIHL VEALPIVLNM FEKKLSSYAQ SHLENTSIKV
310 320 330 340 350 360
HLRTAVAKVE EKQLLAKTKH EDGKITEETI PYGTLIWATG NKARPVITDL FKKIPEQNSS
370 380 390 400 410 420
KRGLAVNDFL QVKGSNNIFA IGDNAFAGLP PTAQVAHQEA EYLAKNFDKM AQIPNFQKNL
430 440 450 460 470 480
SSRKDKIDLL FEENNFKPFK YNDLGALAYL GSERAIATIR SGKRTFYTGG GLMTFYLWRI
490 500 510
LYLSMILSAR SRLKVFFDWI KLAFFKRDFF KGL