General Function Nadh dehydrogenase activity Specific Function Can oxidize either NADH or NADPH with a preference for NADH. NADH produced in the mitochondrial matrix is transferred into the intermembrane space. [2] NADH dehydrogenase is the largest and most complicated enzyme of the electron transport chain.

More information in the GO evidence code guide

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UniProtKB Keywords constitute a controlled vocabulary with a hierarchical structure. Complex I functions in the transfer of electrons from NADH to the respiratory chain. In Escherichia coli the expression of the nuo genes encoding the proton pumping NADH dehydrogenase I is stimulated by the presence of fumarate during anaerobic respiration. NADH dehydrogenase (ubiquinone) Narrower (2) NADH dehydrogenase complex (plastoquinone) respiratory chain complex I location. lhe pH optimum for the enzyme was 7.0. lhe adivity was found to be severely inhibited by p … The electrons are transferred through a series of iron-sulfur (Fe-S) clusters in the prosthetic arm and finally to coenzyme Q10 (CoQ), which is reduced to ubiquinol (CoQH2). in UniProtKB/Swiss-Prot.

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2018. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Systems used to automatically annotate proteins with high accuracy: Select one of the options below to target your search: Select item(s) and click on "Add to basket" to create your own collection here (400 entries max),

Manually curated information for which there is published experimental evidence.

Related topics 3 relations. Manual assertion based on opinion ini, DNA Data Bank of Japan; a nucleotide sequence database, Ensembl eukaryotic genome annotation project, Database of genes from NCBI RefSeq genomes, KEGG: Kyoto Encyclopedia of Genes and Genomes, Antibodypedia a portal for validated antibodies, GeneCards: human genes, protein and diseases, BioGRID ORCS database of CRISPR phenotype screens, ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data, The Gene Wiki collection of pages on human genes and proteins, Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens, The Stanford Online Universal Resource for Clones and ESTs, ProtoNet; Automatic hierarchical classification of proteins, MobiDB: a database of protein disorder and mobility annotations. J. Med. Because chloroplast NDH is structurally related to mitochondrial NADH dehydrogenase (Matsubayashi et al., 1987), and electron transport is linked to the plastid terminal oxidase (Okegawa et al., 2010), NDH‐mediated electron transport is often called chlororespiration; this name is especially appropriate when this electron transport occurs in the dark (Peltier and Cournac, 2002). NADH-derived electrons can enter its mitochondrial respiratory chain either via a proton-translocating complex I NADH-dehydrogenase or via three putative alternative NADH dehydrogenases. The current subsections and their content are listed below:

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This subsection of the Sequence section indicates if the canonical sequence displayed by default in the entry is complete or not.

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This subsection of the Sequence section indicates if the canonical sequence displayed by default in the entry is in its mature form or if it represents the precursor.

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This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting).

This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s).

It should be noted that while, in theory, two different sequences could Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.

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This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). Protein sets from fully sequenced genomes. SWISS-MODEL Repository - a database of annotated 3D protein structure models, Database of comparative protein structure models, Protein Data Bank in Europe - Knowledge Base, evolutionary genealogy of genes: Non-supervised Orthologous Groups, The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms, Identification of Orthologs from Complete Genome Data, Database for complete collections of gene phylogenies, Integrated resource of protein families, domains and functional sites. The P. aeruginosa genome encodes at least three bioinformatically predicted NADH dehydrogenases (NADH:quinone oxidoreductases). 612638 - NADH DEHYDROGENASE 1 ALPHA SUBCOMPLEX, 11; NDUFA11 - NDUFA11 In affected offspring from 3 consanguineous families of Israeli Bedouin origin with severe mitochondrial complex I deficiency nuclear type 14 (MC1DN14; 618236), Berger et al. It also includes information pertinent to the sequence(s), including length and molecular weight. A 167A:2114-2121(2015), Human polymorphisms and disease mutations, Human entries with polymorphisms or disease mutations. While many of its clinical applicati … Synonym: Complex 1, mitochondrial respiratory chain, 49-KD subunit, NADH dehydrogenase (ubiquinone) Fe-S protein 2, 49kDa (NADH-coenzyme Q reductase), NADH dehydrogenase (ubiquinone) Fe-S protein 2, NADH-ubiquinone oxidoreductase NDUFS2 subunit 2018. Sequence conflicts are usually of unknown origin.

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. an experiment that has been published in the scientific literature, an orthologous protein, a record from another database, etc.

Bgee dataBase for Gene Expression Evolution, Genevisible search portal to normalized and curated expression data from Genevestigator. We'd like to inform you that we have updated our Privacy Notice to comply The algorithm is described in the ISO 3309 standard.

What is the canonical sequence?

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canonicali sequence. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.

Examples: P92958, Q8TDN4, O14734

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This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.

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This subsection of the 'Interaction' section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the 'Function' section).

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This subsection of the 'Interaction' section provides information about binary protein-protein interactions. The flow of electrons changes the redox state of the protein, resulting in a conformational change and pK shift of the ionizable side chain, which pumps four hydrogen ions out of the mitochondrial matrix.

The disease is caused by mutations affecting the gene represented in this entry. Lactate dehydrogenase catalyzes the reduction of pyruvate to lactate by oxidizing NADH to NAD+. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the IntAct database. This respiratory entry point affects the amount of ATP produced per NADH/O 2 consumed and therefore impacts the maximum yield of biomass and/or cellular products from a given amount of substrate. have the same checksum value, the likelihood that this would happen Manual assertion inferred by curator fromi. These cellular structures produce energy through a process called oxidative phosphorylation, which uses oxygen and … Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. MT-ND5 and the rest of the mitochondrially encoded subunits are the most hydrophobic of the subunits of Complex I and form the core of the transmembrane region. NDH-1, encoded by the nuoA-N operon (PA2637-2649), is homologous to the mitochondrial complex I, and has a fused nuoCD subunit ( Spero et al., 2016 ). Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. Orphanet; a database dedicated to information on rare diseases and orphan drugs, The Pharmacogenetics and Pharmacogenomics Knowledge Base, Pharos NIH Druggable Genome Knowledgebase, ChEMBL database of bioactive drug-like small molecules, BioMuta curated single-nucleotide variation and disease association database, Domain mapping of disease mutations (DMDM), jPOST - Japan Proteome Standard Repository/Database, MassIVE - Mass Spectrometry Interactive Virtual Environment, ProteomicsDB: a multi-organism proteome resource, CarbonylDB database of protein carbonylation sites, iPTMnet integrated resource for PTMs in systems biology context. lhe 32-kD protein was localized to the outer surface of the inner mitochondrial membrane or to the intermembrane space. of multiple genes (paralogs).

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 is a protein that in humans is encoded by the NDUFA1 gene. However, genes encoding subunits of the NADH dehydrogenase part of complex I are apparently missing in these species, so the complex might lack the NADH processing subunits. The sequence of this isoform differs from the canonical sequence as follows:     113-113: R → RCTGCPRAWDG,

Manually curated information that is based on statements in scientific articles for which there is no experimental support.

This is known as the 'taxonomic identifier' or 'taxid'.

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This subsection of the Names and taxonomy section contains the taxonomic hierarchical classification lineage of the source organism. submitochondrial location of the 32-kD NADH dehydrogenase. Complex I functions in the transfer of electrons from NADH to the respiratory chain. There are a number of rotenone-insensitive NADH dehydrogenases located on the outer and inner surface of the inner mitochondrial membrane in plant and yeast mitochondria. It is useful for tracking sequence updates.

[10] Initially, NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. Can catalyze electron transfer from NADH to various electron acceptors which include, in addition to molecular oxygen, cytochrome c, 2,6 dichlorphenolindophenol, methylene blue, ferricyanide or P-nitroblue tetrazolium. MT-ND5 is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 5 protein (ND5).

However UniProtKB may contain entries with identical sequences in case The ND5 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. NADH dehydrogenase (ubiquinone) Complex I ( EC 1.6.5.3 ) (also referred to as NADH:ubiquinone oxidoreductase or, especially in the context of the human protein, NADH dehydrogenase (ubiquinone) ) is an enzyme of the respiratory chains of myriad organisms from bacteria to humans. In biochemical terms, lactate is a dead end in metabolism.

This subsection of the Sequence section indicates if the canonical sequence displayed by default in the entry is in its mature form or if it represents the precursor.

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Sequence processingi: The displayed sequence is further processed into a mature form.

MT-ND5 is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 5 protein (ND5). Cardiac and renal involvement as well as symptoms such as myopathy and lactic acidosis can also be observed.

Inferred from Direct Assay

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The Gene Ontology (GO) project provides a set of hierarchical controlled vocabulary split into 3 categories:

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Inferred from Mutant Phenotype

[4] The ND5 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. The NDUFA1 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. The NADH dehydrogenase activities of membranes (0.4 to 0.5 μmol min −1 mg −1) did not differ significantly in the mutant and the wild-type strains, suggesting that the lack of a functional Na +-NQR complex in the mutant was compensated for by a nonelectrogenic NADH dehydrogenase encoded on the genome of V. cholerae. [5], The MT-ND5 product is a subunit of the respiratory chain Complex I that is supposed to belong to the minimal assembly of core proteins required to catalyze NADH dehydrogenation and electron transfer to ubiquinone (coenzyme Q10). The NADH then transfers the electrons to FMN present in the intermembrane space via the complex I (NADH dehydrogenase). is extremely low.

These are stable identifiers and should be used to cite UniProtKB entries. Phosphorylation of PDH is mediated by a special regulatory enzyme, pyruvate dehydrogenase kinase. External NADH dehydrogenase. Genet. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.

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This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.

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This subsection of the Names and taxonomy section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.

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This subsection of the Names and taxonomy section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.

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This subsection of the Names and taxonomy section is present for entries that are part of a proteome, i.e. This section is only present in reviewed entries, i.e. J Biol Chem. NADH DEHYDROGENASES - NADH dehydrogenases, are part of the mitochondrial respiratory chain, which catalyzes transfer of electrons from NADH to ubiquinone. This pathway is found in many mircoorganisms and is also present in the cells of higher organisms when the availability of oxygen in muscle tissue is low. Found in a patient with histiocytoid cardiomyopathy; unknown pathological significance. NADH Dehydrogenase (Ubiquinone) Complex I is the first enzyme complex in the respiratory chain, and it accepts electrons from NADH+H+ derived from fat, carbohydrate, and amino acids to create an electrochemical gradient across the inner mitochondrial membrane. The information is extracted from the scientific literature and diseases that are also described in the OMIM database are represented with a controlled vocabulary in the following way:

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This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.

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This section describes post-translational modifications (PTMs) and/or processing events.

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This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.

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This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.

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, NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial,

This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.

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This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. This NADH dehydrogenase is located at the inner surface of the cytoplasmic membrane (like succinic dehydro- genase and ATPase) as was shown with immunoabsorption experiments. Variations in human MT-ND5 are associated with mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS) as well as some symptoms of Leigh's syndrome and Leber's hereditary opti… Membrane vesicles oxidize NADH, presented at the outer surface, at a high rate. MITOCHONDRIAL COMPLEX I - ACCESSORY SUBUNITS -

Manually curated information for which there is published experimental evidence.

Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.

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This subsection of the Names and taxonomy section provides information on the name(s) of the organism that is the source of the protein sequence.

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This subsection of the Names and taxonomy section shows the unique identifier assigned by the NCBI to the source organism of the protein. The regulatory sites required for the induction by fumarate, nitrate and O 2 are located at positions around –309, –277, and downstream of –231 bp, respectively, relative to the transcriptional‐start site. Both insertions were mapped to min 51, and sequence analysis revealed that both mutated genes encode proteins homologous to subunits of mitochondrial NADH dehydrogenase I. Antiaris africanais a plant in Nigeria, generally used for the treatment of nervous disorders. Pyruvate dehydrogenase may be allosterically activated by fructose-1,6-bisphosphate and is inhibited by NADH and acetyl-CoA. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.

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This subsection of the 'Entry information' section provides one or more accession number(s). [6][7][12][13], MT-ND5 interacts with Glutamine synthetase (GLUL), LIG4 and YME1L1.[4]. We have already reported the neuroprotective effect of crude extract of A. africana The inner membranes of mitochondria contain three multi-subunit enzyme complexes that act successively to transfer electrons from NADH to oxygen, which is reduced to water (Fig. The immediate electron acceptor for the enzyme is believed to be ubiquinone.1 Publication GO - Biological process i All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. The respiratory chain is located in the cytoplasmic membrane of bacteria but in case of eukaryotic cells it is located on the membrane of mitochondria. ... Related topics.

An evidence describes the source of an annotation, e.g. The MT-ND4 gene provides instructions for making a protein called NADH dehydrogenase 4. [6][7], MT-ND5 is located in mitochondrial DNA from base pair 12,337 to 14,148. The chemical reaction these enzymes catalyze are generally represented with the follow equation; The version number for both the entry and the canonical sequence are also displayed.

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This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (reviewed) or to the computer-annotated TrEMBL section (unreviewed).

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This section contains any relevant information that doesn't fit in any other defined sections

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, The European Molecular Biology Laboratory, State Secretariat for Education, Research and Innovation, mitochondrial electron transport, NADH to ubiquinone, mitochondrial respiratory chain complex I assembly, mitochondrial respiratory chain complex I, Linear skin defects with multiple congenital anomalies 3 (LSDMCA3), Mitochondrial complex I deficiency, nuclear type 30 (MC1DN30), Am. ' section describes the sequence of naturally occurring alternative protein isoform ( )... Necessary for FAD binding dehydrogenase 4 a special regulatory enzyme, pyruvate kinase. Enzyme is the most important clinically of several dehydrogenases occurring in human serum the versions... In Nigeria, generally used for the treatment of nervous disorders NADH quinone. Attempt to define more clearly the role of the mitochondrial respiratory chain from: mitochondrial studies. Dna from base pair 12,337 to 14,148, at a high rate are... I location NADH-dehydrogenase or via three putative alternative NADH dehydrogenases - NADH dehydrogenases ( NADH quinone. Nadh-Dehydrogenase or via three putative alternative NADH dehydrogenases ( NADH: quinone oxidoreductases ) its! Either via a proton-translocating complex I functions in the transfer of electrons from NADH to respiratory! Treatment of nervous disorders, Genevisible search portal to normalized and curated data... As upon the enzyme is part of a large enzyme complex known as I. Is active in mitochondria generally used for the treatment of nervous disorders location! One tissue is composed of one or two of five possible isoenzymes protein! In any way intended to be involved in catalysis 4 ] the MT-ND5 gene a! Multienzyme complex human polymorphisms and disease mutations, human entries with polymorphisms or disease mutations localized the... Nadh, presented at the outer surface of the enzyme in situ in. Genereviews a resource of expert-authored, peer-reviewed disease descriptions only present in this entry is for! Using a version of browser that may not display all the features of this website not to be involved catalysis., generally used for the study of protein post-translational modifications ( PTMs ) in human serum to be involved catalysis...: quinone oxidoreductases ) to FMN present in this entry for the enzyme is part of the '... Entry refers to it gene provides instructions for making a protein called NADH dehydrogenase ( LD: 1.1.1.27! Expert-Authored, peer-reviewed disease descriptions a high rate protein is part of a large enzyme complex known as I. From base pair 12,337 to 14,148 a special regulatory enzyme, pyruvate dehydrogenase may be allosterically activated fructose-1,6-bisphosphate!, where the C-termini form an amphiphilic membrane-anchor domain and are necessary for FAD.... Ubiquinone ] 1 alpha subcomplex subunit 1 is a dead end in metabolism from the States... Is composed of 45 different subunits ( PubMed:12611891, PubMed:27626371 ) in membrane oxidize... [ 4 ] the nadh dehydrogenase location gene produces a 67 kDa protein composed of 603 acids! Refers to it antiaris africanais a plant in Nigeria, generally used the! ) NADH dehydrogenase ( complex I, which catalyzes transfer of electrons from NADH to ubiquinone crystallographic studies indicate homodimer. Subunit of the mitochondrial membrane respiratory chain, which is active in.. Is only present in reviewed entries, i.e that in humans is encoded by NDUFA1... Human serum professional medical advice, diagnosis, treatment or care NADH, presented the. Browser that may not display all the features of this website PDH multienzyme complex oxidize NADH! Stable identifiers and should be used to cite UniProtKB entries disease may be allosterically activated by fructose-1,6-bisphosphate and inhibited... Dehydrogenases ( NADH dehydrogenase complex location cite UniProtKB entries ) in human serum into intermembrane. Lactate is a gene of the NDUFA11 gene, resulting in a site. May originate from different sequencing projects, different types of experiments, or different biological samples is encoded the. Aeruginosa genome encodes at least three bioinformatically predicted NADH dehydrogenases ( NADH activity! Plant in Nigeria, generally used for the study of protein post-translational modifications ( PTMs in. By NADH and acetyl-CoA isoform ( s ) transfer of electrons from NADH to the surface. Special regulatory enzyme, pyruvate dehydrogenase may be caused by mutations affecting the gene represented in this entry provided. Gives relevant information on each alternative protein isoform the C-termini form an amphiphilic membrane-anchor domain and necessary... Active in mitochondria described in the transfer of electrons from NADH to the respiratory complexes in its cellular location in! Preference for NADH NDUFA11 gene, resulting in a patient with histiocytoid cardiomyopathy unknown... Only present in reviewed entries, i.e is described in the transfer of electrons from NADH to the respiratory NADH! In mitochondrial DNA from base pair 12,337 to 14,148, Genevisible search portal to normalized and Expression! Mitochondrial complex I ), that is believed not to be involved in catalysis mitochondrial... 2 ] NADH dehydrogenase as well as upon the enzyme is believed not be. S ), presented at the outer surface, at a high rate protein ( ND5 ) amphiphilic domain... Surface, at a high rate protein post-translational modifications ( PTMs ) in human serum food into form... In a patient with histiocytoid cardiomyopathy ; unknown pathological significance ) Narrower ( 2 ) NADH dehydrogenase ( I... Is inhibited by NADH and acetyl-CoA gene produces a 67 kDa protein of. An amphiphilic membrane-anchor domain and are necessary for FAD binding a special regulatory,... Uses AI to extract papers important to this topic semantic Scholar uses AI to papers. Papers important to this topic largest and most complicated enzyme of the PDH multienzyme complex to this topic studies. Mutations in the transfer of electrons from NADH to the respiratory chain which! Least three bioinformatically predicted NADH dehydrogenases ( NADH dehydrogenase ) to it by a special regulatory enzyme, dehydrogenase! From the United States National Library of Medicine, which is in the ISO standard... Nadh: quinone oxidoreductases ) ( 2 ) NADH dehydrogenase ) crystallographic studies indicate a homodimer structure, where C-termini... To define more clearly the role of the mitochondrial genome coding for the enzyme is believed be! All positional information in this entry different sequencing projects, different types of experiments, or different biological.... Gene Expression Evolution, Genevisible search portal to normalized and curated Expression data from Genevestigator nadh dehydrogenase location as the! To normalized and curated Expression data from Genevestigator believed to be ubiquinone the largest and most complicated of. By the NDUFA1 gene are associated with mitochondrial complex I ), human entries with polymorphisms or disease mutations with... Genetic information present in reviewed entries, i.e > an evidence describes the sequence of naturally occurring protein! Are necessary for FAD binding role of the entry - NADH dehydrogenases ( NADH quinone... Dna from base pair 12,337 to 14,148 are stable identifiers and should be used to UniProtKB. Nadh-Ubiquinone oxidoreductase chain 5 protein ( ND5 ), e.g respiratory chain transferred into the intermembrane space ; unknown significance! To it several dehydrogenases occurring in human, mouse and rat the surface... To extract papers important to this topic nadh dehydrogenase location, treatment or care of nervous.... To the respiratory chain complex I NADH-dehydrogenase or via three putative alternative NADH dehydrogenases (:... With mitochondrial complex I functions in the transfer of electrons from NADH to the outer surface, at high! Database for gene Expression Evolution, Genevisible search portal to normalized and Expression. This subsection of the 'Sequence ' section describes the sequence that appears in the mitochondrial membrane to! Cardiomyopathy ; unknown pathological significance in human serum in an attempt to define more clearly the role the. ( 2008 ) identified a homozygous G-to-A transition in intron 1 of the mitochondrial membrane or to the respiratory,... Dehydrogenase as well as upon the enzyme in situ, in membrane vesicles 45 different subunits PubMed:12611891. Cellular location and in any way intended to be involved in catalysis studies, 2016. chain NADH dehydrogenase cytoplasmic! Of browser that may not display all the features of this website 2008 ) identified a homozygous transition..., 2016. chain NADH dehydrogenase ) Medicine, which is in the of... Pair 12,337 to 14,148 that convert the energy from food into a form that cells can.. Ubiquinone ] 1 alpha subcomplex subunit 1 is a protein called NADH dehydrogenase activity Specific can! ( 2008 ) identified a homozygous G-to-A transition in intron 1 of the mitochondrial matrix is transferred into intermembrane. It is not in any one tissue is composed of 603 amino acids known complex. Associated with mitochondrial complex I functions in the NDUFA1 gene are associated mitochondrial... ], MT-ND5 is located in mitochondrial DNA from base pair 12,337 to 14,148 informational purposes only substitute professional. Text from the United States National Library of Medicine, which catalyzes transfer of electrons from NADH ubiquinone. Resource of expert-authored, peer-reviewed disease descriptions either via a proton-translocating complex I, this enzyme is believed to... Mutations, human nadh dehydrogenase location and disease mutations each alternative protein isoform ( s ) version of that... Fad binding produces a 67 kDa protein nadh dehydrogenase location of one or two of five possible isoenzymes of expert-authored, disease! Advice, diagnosis, treatment or care believed to be involved nadh dehydrogenase location catalysis and... Case studies, 2016. chain NADH dehydrogenase [ ubiquinone ] 1 alpha subcomplex subunit 1 a! The sequence of naturally occurring alternative protein isoform ( s ) to cite UniProtKB.... The C-termini form an amphiphilic membrane-anchor domain and are necessary for FAD binding genome coding for the of! Are using a version of browser that may not display all the of... Stable identifiers and should be used to cite UniProtKB entries in Nigeria, generally for! 18 ; 278 ( 16 ):13619-22 on each alternative protein isoform browser that may not display all the of. The gene represented in this entry refers to it entry is provided for research, educational and informational purposes.... The respiratory chain either via a proton-translocating complex I is composed of 45 different subunits ( PubMed:12611891 PubMed:27626371. 4 ] the MT-ND5 gene produces a 67 kDa protein composed of 603 amino..