Q95H42

PR
Gene name
ndhH
Protein name
NAD(P)H-quinone oxidoreductase subunit H, chloroplastic
Names
NAD(P)H dehydrogenase subunit H, NADH-plastoquinone oxidoreductase 49 kDa subunit, NADH-plastoquinone oxidoreductase subunit H
Species
Triticum aestivum (Wheat)
KEGG Pathway
taes:803138
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

264-344 (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 Q95H42

Entry ID Method Resolution Chain Position Source
AF-Q95H42-F1 Predicted AlphaFoldDB

No variants for Q95H42

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q95H42

No associated diseases with Q95H42

2 regional properties for Q95H42

Type Name Position InterPro Accession
domain NADH-quinone oxidoreductase, subunit D 124 - 393 IPR001135
conserved_site NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site 47 - 58 IPR014029

Functions

Description
EC Number
Subcellular Localization
  • Plastid, chloroplast thylakoid membrane ; Peripheral membrane protein ; Stromal side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
chloroplast thylakoid membrane The pigmented membrane of a chloroplast thylakoid. An example of this component is found in Arabidopsis thaliana.

3 GO annotations of molecular function

Name Definition
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.
NADH dehydrogenase (ubiquinone) activity Catalysis of the reaction: NADH + ubiquinone + 5 H(+)(in) <=> NAD(+) + ubiquinol + 4 H(+)(out).
quinone binding Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds.

1 GO annotations of biological process

Name Definition
photosynthesis, light reaction The light reactions of photosynthesis, which take place in photosystems II and I. Light energy is harvested and used to power the transfer of electrons among a series of electron donors and acceptors. The final electron acceptor is NADP+, which is reduced to NADPH. NADPH generated from light reactions is used in sugar synthesis in dark reactions. Light reactions also generate a proton motive force across the thylakoid membrane, and the proton gradient is used to synthesize ATP. There are two chemical reactions involved in the light reactions: water oxidation in photosystem II, and NADP reduction in photosystem I.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P25709 ndhH NAD(P)H-quinone oxidoreductase subunit H, chloroplastic Zea mays (Maize) PR
A4GYX2 ndhH NAD(P)H-quinone oxidoreductase subunit H, chloroplastic Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) PR
Q2VEC5 ndhH NAD(P)H-quinone oxidoreductase subunit H, chloroplastic Solanum tuberosum (Potato) PR
P0C337 ndhH NAD(P)H-quinone oxidoreductase subunit H, chloroplastic Oryza sativa subsp japonica (Rice) PR
Q93873 gas-1 Probable NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial Caenorhabditis elegans PR
A1E9Y0 ndhH NAD(P)H-quinone oxidoreductase subunit H, chloroplastic Sorghum bicolor (Sorghum) (Sorghum vulgare) PR
P56753 ndhH NAD(P)H-quinone oxidoreductase subunit H, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
Q2MI44 ndhH NAD(P)H-quinone oxidoreductase subunit H, chloroplastic Solanum lycopersicum (Tomato) (Lycopersicon esculentum) PR
10 20 30 40 50 60
MSLPLTRKDL MIVNMGPQHP SMHGVLRLIV TLDGEDVIDC EPILGYLHRG MEKIAENRTI
70 80 90 100 110 120
IQYLPYVTRW DYLATMFTEA ITVNAPEFLE NIQIPQRASY IRVIMLELSR IASHLLWLGP
130 140 150 160 170 180
FMADLGAQTP FFYIFREREL IYDLFEAATG MRMMHNYFRI GGVAADLPYG WIEKCLDFCD
190 200 210 220 230 240
YFLRGVVEYQ QLITQNPIFL ERVEGVGFIS GEEAVNWGLS GPMLRASGIQ WDLRKVDPYE
250 260 270 280 290 300
SYNQFDWKVQ WQKEGDSLAR YLVRVGEMRE SIKIIQQAVE KIPGGPYENL EVRRFKKEKN
310 320 330 340 350 360
SEWNDFEYKF LGKKPSPNFE LSRQELYVRV EAPKGELGIY LVGDDSLFPW RWKIRPPGFI
370 380 390
NLQILPQLVK KMKLADIMTI LGSIDIIMGE VDR