LTO1 NAD(P)H dehydrogenase (quinone)s [Arabidopsis thaliana (thale cress)] - Gene

Summary

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Official Symbol: LTO1
Official Full Name: NAD(P)H dehydrogenase (quinone)s
Primary source: TAIR:AT4G35760
Locus tag: AT4G35760
See related: Araport:AT4G35760
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Arabidopsis thaliana (ecotype: Columbia)
Lineage: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis
Also known as: F4B14.2; Lumen Thiol Oxidoreductase 1
Summary: Encodes a bimodular enzyme comprising an integral domain homologous to the catalytic subunit of mammalian vitamin K epoxide reductase (VKORC1, EC 1.1.4.1) that is fused to a soluble thioredoxin-like moiety. Using yeast microsomes as a recombinant system, it was shown that the VKORC1 domain of At4g35760 functions as a stringent naphthoquinone reductase, and that its reduced Trx-like partner can serve as its electron donor. Located in plastid. Required for the assembly of photosystem II. Can catalyze disulfide bond formation in vitro.
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Genomic context

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See LTO1 in Genome Data Viewer

Location:: chromosome: 4

Exon count:: 7

Sequence:: Chromosome: 4; NC_003075.7 (16942031..16944677, complement)

Chromosome 4 - NC_003075.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003075.7

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7.
Title: Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7.
involved in abscisic acid-mediated response to osmotic stress
Title: Thylakoid membrane oxidoreductase LTO1/AtVKOR is involved in ABA-mediated response to osmotic stress in Arabidopsis.
Results identified HCF164 as a direct target of LTO1 interacting with its thioredoxin-like domain suggesting that VKOR may play an important role in regulating the redox state of proteins in the thylakoid lume.
Title: Identification of potential targets for thylakoid oxidoreductase AtVKOR/LTO1 in chloroplasts.
The conserved cysteines in the AtVKOR domain also played critical roles in phylloquinone reduction. When each of the four conserved cysteines was mutated to alanine, the mutants lost reduction activity entirely.
Title: Key amino acids of arabidopsis VKOR in the activity of phylloquinone reduction and disulfide bond formation.
LTO1 is involved in the xanthophyll cycle and the acceleration of D1 protein degradation.
Title: The chloroplast protein LTO1/AtVKOR is involved in the xanthophyll cycle and the acceleration of D1 protein degradation.
Lumen Thiol Oxidoreductase1 (LTO1) is a disulfide bond-forming enzyme in the thylakoid lumen. Loss of LTO1 produces a photosynthetic defect.[LTO1]
Title: Lumen Thiol Oxidoreductase1, a disulfide bond-forming catalyst, is required for the assembly of photosystem II in Arabidopsis.
LTO1 plays important roles in redox regulation, ROS homeostasis and maintenance of PSII.
Title: A chloroplast membrane protein LTO1/AtVKOR involving in redox regulation and ROS homeostasis.
characterization of protein encoded by At4g35760 as disulfide bond oxidoreductase with 2 distinct domains (membrane domain homologous to catalytic subunit of VKOR and soluble DsbA-like domain) with protein sorting signal that targets to thylakoids
Title: A protein oxidase catalysing disulfide bond formation is localized to the chloroplast thylakoids.
The VKORC1 domain of At4g35760 functions as a stringent naphthoquinone reductase, and that its reduced thioredoxin-like partner can serve as its electron donor.
Title: A bimodular oxidoreductase mediates the specific reduction of phylloquinone (vitamin K₁) in chloroplasts.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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NM_001342367.1

Supported by ESTs:

NM_119742.4

Supported by ESTs:

Gene Ontology Provided by TAIR

Function	Evidence Code	Pubs
enables NAD(P)H dehydrogenase (quinone) activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
acts_upstream_of_or_within photosystem II assembly	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in chloroplast	HDA more info	PubMed
located_in chloroplast	ISM Inferred from Sequence Model more info
located_in plastid	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: NAD(P)H dehydrogenase (quinone)s

NP_567988.1

NAD(P)H dehydrogenase (quinone)s; FUNCTIONS IN: NAD(P)H dehydrogenase (quinone) activity; LOCATED IN: chloroplast, plastid; EXPRESSED IN: 23 plant structures; EXPRESSED DURING: 13 growth stages; CONTAINS InterPro DOMAIN/s: Vitamin K epoxide reductase (InterPro:IPR012932), Thioredoxin-like fold (InterPro:IPR012336); Has 30201 Blast hits to 17322 proteins in 780 species: Archae - 12; Bacteria - 1396; Metazoa - 17338; Fungi - 3422; Plants - 5037; Viruses - 0; Other Eukaryotes - 2996 (source: NCBI BLink).

NCBI Reference Sequences (RefSeq)

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Genome Annotation

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Reference assembly

Genomic

NC_003075.7 Reference assembly

Range

16942031..16944677 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_119742.4 → NP_567988.1 NAD(P)H dehydrogenase (quinone)s [Arabidopsis thaliana]

See identical proteins and their annotated locations for NP_567988.1

Status: REVIEWED

UniProtKB/Swiss-Prot

O81807, Q8L540, Q8L9V9

UniProtKB/TrEMBL

A0A178V2Y0, A0A5S9XYY3

Conserved Domains (2) summary

cd12916
Location:80 → 202

VKOR_1; Vitamin K epoxide reductase family in bacteria and plants

cl00388
Location:286 → 359

Thioredoxin_like; Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold
NM_001342367.1 → NP_001329911.1 NAD(P)H dehydrogenase (quinone)s [Arabidopsis thaliana]

Status: REVIEWED

UniProtKB/TrEMBL

A0A1P8B950, A0A5S9XYY3