Type |
Details |
Score |
Protein Domain |
|
•
•
•
•
•
|
Publication |
First Author: |
Reinard T |
Title: |
Cloning of a gene for an acyl-CoA dehydrogenase from Pisum sativum L. and purification and characterization of its product as an isovaleryl-CoA dehydrogenase. |
Year: |
2000 |
Journal: |
J Biol Chem |
Volume: |
275 |
Pages: |
33738-43 |
|
•
•
•
•
•
|
Publication |
First Author: |
Rognes SE |
Title: |
Transcriptional and biochemical regulation of a novel Arabidopsis thaliana bifunctional aspartate kinase-homoserine dehydrogenase gene isolated by functional complementation of a yeast hom6 mutant. |
Year: |
2003 |
Journal: |
Plant Mol Biol |
Volume: |
51 |
Pages: |
281-94 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kotchoni SO |
Title: |
Over-expression of different aldehyde dehydrogenase genes in Arabidopsis thaliana confers tolerance to abiotic stress and protects plants against lipid peroxidation and oxidative stress. |
Year: |
2006 |
Journal: |
Plant Cell Environ |
Volume: |
29 |
Pages: |
1033-48 |
|
•
•
•
•
•
|
Publication |
First Author: |
Cousins AB |
Title: |
Peroxisomal malate dehydrogenase is not essential for photorespiration in Arabidopsis but its absence causes an increase in the stoichiometry of photorespiratory CO2 release. |
Year: |
2008 |
Journal: |
Plant Physiol |
Volume: |
148 |
Pages: |
786-95 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lin M |
Title: |
Disruption of plE2, the gene for the E2 subunit of the plastid pyruvate dehydrogenase complex, in Arabidopsis causes an early embryo lethal phenotype. |
Year: |
2003 |
Journal: |
Plant Mol Biol |
Volume: |
52 |
Pages: |
865-72 |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhu X |
Title: |
The activity of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is regulated by functional interaction between its two enzyme domains. |
Year: |
2002 |
Journal: |
J Biol Chem |
Volume: |
277 |
Pages: |
49655-61 |
|
•
•
•
•
•
|
Publication |
First Author: |
Honeyman AL |
Title: |
Isolation, characterization, and nucleotide sequence of the Streptococcus mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific factor III gene of the phosphoenolpyruvate phosphotransferase system. |
Year: |
1992 |
Journal: |
Infect Immun |
Volume: |
60 |
Pages: |
3369-75 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mukhopadhyay B |
Title: |
Cloning, sequencing, and transcriptional analysis of the coenzyme F420-dependent methylene-5,6,7,8-tetrahydromethanopterin dehydrogenase gene from Methanobacterium thermoautotrophicum strain Marburg and functional expression in Escherichia coli. |
Year: |
1995 |
Journal: |
J Biol Chem |
Volume: |
270 |
Pages: |
2827-32 |
|
•
•
•
•
•
|
Publication |
First Author: |
Delforge D |
Title: |
Similarities between alanine dehydrogenase and the N-terminal part of pyridine nucleotide transhydrogenase and their possible implication in the virulence mechanism of Mycobacterium tuberculosis. |
Year: |
1993 |
Journal: |
Biochem Biophys Res Commun |
Volume: |
190 |
Pages: |
1073-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Faure M |
Title: |
Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structures of H- and L-proteins. |
Year: |
2000 |
Journal: |
Eur J Biochem |
Volume: |
267 |
Pages: |
2890-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jeon WB |
Title: |
Purification and characterization of membrane-associated CooC protein and its functional role in the insertion of nickel into carbon monoxide dehydrogenase from Rhodospirillum rubrum. |
Year: |
2001 |
Journal: |
J Biol Chem |
Volume: |
276 |
Pages: |
38602-9 |
|
•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Publication |
First Author: |
Smith C |
Title: |
Alterations in the mitochondrial alternative NAD(P)H Dehydrogenase NDB4 lead to changes in mitochondrial electron transport chain composition, plant growth and response to oxidative stress. |
Year: |
2011 |
Journal: |
Plant Cell Physiol |
Volume: |
52 |
Pages: |
1222-37 |
|
•
•
•
•
•
|
Publication |
First Author: |
Conley TR |
Title: |
Characterization of cis-acting elements in light regulation of the nuclear gene encoding the A subunit of chloroplast isozymes of glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana. |
Year: |
1994 |
Journal: |
Mol Cell Biol |
Volume: |
14 |
Pages: |
2525-33 |
|
•
•
•
•
•
|
Publication |
First Author: |
Nakashima K |
Title: |
A gene encoding proline dehydrogenase is not only induced by proline and hypoosmolarity, but is also developmentally regulated in the reproductive organs of Arabidopsis. |
Year: |
1998 |
Journal: |
Plant Physiol |
Volume: |
118 |
Pages: |
1233-41 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hochheimer A |
Title: |
The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme. |
Year: |
1998 |
Journal: |
Arch Microbiol |
Volume: |
170 |
Pages: |
389-93 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lyon EJ |
Title: |
Carbon monoxide as an intrinsic ligand to iron in the active site of the iron-sulfur-cluster-free hydrogenase H2-forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy. |
Year: |
2004 |
Journal: |
J Am Chem Soc |
Volume: |
126 |
Pages: |
14239-48 |
|
•
•
•
•
•
|
Publication |
First Author: |
Benachenhou-Lahfa N |
Title: |
Evolution of glutamate dehydrogenase genes: evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life. |
Year: |
1993 |
Journal: |
J Mol Evol |
Volume: |
36 |
Pages: |
335-46 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mennenga B |
Title: |
Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550. |
Year: |
2009 |
Journal: |
Arch Microbiol |
Volume: |
191 |
Pages: |
361-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Combe JP |
Title: |
Lys-D48 is required for charge stabilization, rapid flavin reduction, and internal electron transfer in the catalytic cycle of dihydroorotate dehydrogenase B of Lactococcus lactis. |
Year: |
2006 |
Journal: |
J Biol Chem |
Volume: |
281 |
Pages: |
17977-88 |
|
•
•
•
•
•
|
Publication |
First Author: |
Anderson NA |
Title: |
Manipulation of Guaiacyl and Syringyl Monomer Biosynthesis in an Arabidopsis Cinnamyl Alcohol Dehydrogenase Mutant Results in Atypical Lignin Biosynthesis and Modified Cell Wall Structure. |
Year: |
2015 |
Journal: |
Plant Cell |
Volume: |
27 |
Pages: |
2195-209 |
|
•
•
•
•
•
|
GeneRIF (Gene Reference into Function) |
Annotation: |
Transcriptomic analyses revealed that two genes involved in low-oxygen tolerance, namely GLUTAMATE DEHYDROGENASE 1 (GDH1) and GDH2, showed lower expression levels in the stop1 mutant than in the wild-type. Sensitivity of the gdh1gdh2 double-mutant to low-oxygen conditions was partly attributable to the low-oxygen sensitivity of the stop1 mutant. |
Organism: |
A. thaliana |
Gene: |
HSFA2 |
PubMed Id: |
30882866 |
|
•
•
•
•
•
|
GeneRIF (Gene Reference into Function) |
Annotation: |
Transcriptomic analyses revealed that two genes involved in low-oxygen tolerance, namely GLUTAMATE DEHYDROGENASE 1 (GDH1) and GDH2, showed lower expression levels in the stop1 mutant than in the wild-type. Sensitivity of the gdh1gdh2 double-mutant to low-oxygen conditions was partly attributable to the low-oxygen sensitivity of the stop1 mutant. |
Organism: |
A. thaliana |
Gene: |
STOP1 |
PubMed Id: |
30882866 |
|
•
•
•
•
•
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Protein Domain |
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•
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•
•
•
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Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
|
•
•
•
•
•
|
GO Term |
Description: |
Catalysis of the reaction: estradiol-17-alpha + NAD(P)+ = estrone + NAD(P)H + H+. |
|
•
•
•
•
•
|
mRNA |
Length: |
1809
![FASTA](model/images/fasta.gif;jsessionid=17CA72ED9DA8AC8182E4F38B7652A6D1) |
Chromosome Location: |
Chr2: 9279931-9282178 |
|
•
•
•
•
•
|
mRNA |
Length: |
1159
![FASTA](model/images/fasta.gif;jsessionid=17CA72ED9DA8AC8182E4F38B7652A6D1) |
Chromosome Location: |
Chr2: 9331058-9332646 |
|
•
•
•
•
•
|
mRNA |
Length: |
1711
![FASTA](model/images/fasta.gif;jsessionid=17CA72ED9DA8AC8182E4F38B7652A6D1) |
Chromosome Location: |
Chr3: 1080942-1083690 |
|
•
•
•
•
•
|
mRNA |
Length: |
1752
![FASTA](model/images/fasta.gif;jsessionid=17CA72ED9DA8AC8182E4F38B7652A6D1) |
Chromosome Location: |
Chr3: 9794862-9797045 |
|
•
•
•
•
•
|
mRNA |
Length: |
1655
![FASTA](model/images/fasta.gif;jsessionid=17CA72ED9DA8AC8182E4F38B7652A6D1) |
Chromosome Location: |
Chr1: 5574257-5577622 |
|
•
•
•
•
•
|
mRNA |
Length: |
2286
![FASTA](model/images/fasta.gif;jsessionid=17CA72ED9DA8AC8182E4F38B7652A6D1) |
Chromosome Location: |
Chr1: 24538886-24542712 |
|
•
•
•
•
•
|
mRNA |
Length: |
1919
![FASTA](model/images/fasta.gif;jsessionid=17CA72ED9DA8AC8182E4F38B7652A6D1) |
Chromosome Location: |
Chr1: 29915902-29919408 |
|
•
•
•
•
•
|
mRNA |
Length: |
1281
![FASTA](model/images/fasta.gif;jsessionid=17CA72ED9DA8AC8182E4F38B7652A6D1) |
Chromosome Location: |
Chr5: 20750513-20752115 |
|
•
•
•
•
•
|
mRNA |
Length: |
1079
![FASTA](model/images/fasta.gif;jsessionid=17CA72ED9DA8AC8182E4F38B7652A6D1) |
Chromosome Location: |
Chr5: 20750513-20752115 |
|
•
•
•
•
•
|
mRNA |
Length: |
867
![FASTA](model/images/fasta.gif;jsessionid=17CA72ED9DA8AC8182E4F38B7652A6D1) |
Chromosome Location: |
Chr5: 20750660-20752023 |
|
•
•
•
•
•
|
mRNA |
Length: |
829
![FASTA](model/images/fasta.gif;jsessionid=17CA72ED9DA8AC8182E4F38B7652A6D1) |
Chromosome Location: |
Chr5: 20750660-20752024 |
|
•
•
•
•
•
|
GO Term |
Description: |
A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). |
|
•
•
•
•
•
|
GO Term |
Description: |
The enzyme, located in the plasma membrane, that catalyzes the oxidation of succinate and ubiquinone to fumarate and ubiquinol; involved in aerobic respiration, repressed in anaerobic respiration. |
|
•
•
•
•
•
|
Protein Domain |
|
•
•
•
•
•
|
GO Term |
Description: |
Catalysis of the reaction: D-glycerate + NADP+ = hydroxypyruvate + NADPH + H+. |
|
•
•
•
•
•
|
GO Term |
Description: |
Catalysis of the reaction: sucrose + acceptor = 3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + reduced acceptor. |
|
•
•
•
•
•
|
GO Term |
Description: |
Catalysis of the reaction: propanoyl-CoA + NAD+ = acryloyl-CoA + H+ + NADH. |
|
•
•
•
•
•
|
GO Term |
Description: |
Catalysis of the reaction: 5-beta-cholestane-3-alpha,7-alpha,12-alpha,26-tetraol + NAD+ = 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-al + NADH. |
|
•
•
•
•
•
|
GO Term |
Description: |
Catalysis of the reaction: D-fructose + A = 5-dehydro-D-fructose + AH(2). |
|
•
•
•
•
•
|
GO Term |
Description: |
Catalysis of the reaction:1-(1,2-saturated alkyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(II)-[cytochrome b5] + 2 H+ + O2 = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(III)-[cytochrome b5] + 2 H2O. |
|
•
•
•
•
•
|
Publication |
First Author: |
Conley TR |
Title: |
Effects of light and chloroplast functional state on expression of nuclear genes encoding chloroplast glyceraldehyde-3-phosphate dehydrogenase in long hypocotyl (hy) mutants and wild-type Arabidopsis thaliana. |
Year: |
1995 |
Journal: |
Plant Physiol |
Volume: |
108 |
Pages: |
1013-22 |
|
•
•
•
•
•
|
Publication |
First Author: |
Popova AV |
Title: |
The intrinsically disordered protein LEA7 from Arabidopsis thaliana protects the isolated enzyme lactate dehydrogenase and enzymes in a soluble leaf proteome during freezing and drying. |
Year: |
2015 |
Journal: |
Biochim Biophys Acta |
Volume: |
1854 |
Pages: |
1517-25 |
|
•
•
•
•
•
|
Publication |
First Author: |
Neidle E |
Title: |
cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. |
Year: |
1992 |
Journal: |
Eur J Biochem |
Volume: |
204 |
Pages: |
113-20 |
|
•
•
•
•
•
|
Publication |
First Author: |
Burton RL |
Title: |
Transient kinetic analysis of the interaction of L-serine with Escherichia coli D-3-phosphoglycerate dehydrogenase reveals the mechanism of V-type regulation and the order of effector binding. |
Year: |
2009 |
Journal: |
Biochemistry |
Volume: |
48 |
Pages: |
12242-51 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hempel J |
Title: |
Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria. |
Year: |
1989 |
Journal: |
Biochemistry |
Volume: |
28 |
Pages: |
1160-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Nishihara M |
Title: |
Purification and properties of sn-glycerol-1-phosphate dehydrogenase from Methanobacterium thermoautotrophicum: characterization of the biosynthetic enzyme for the enantiomeric glycerophosphate backbone of ether polar lipids of Archaea. |
Year: |
1997 |
Journal: |
J Biochem |
Volume: |
122 |
Pages: |
572-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Oubrie A |
Title: |
The 1.7 A crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat. |
Year: |
1999 |
Journal: |
J Mol Biol |
Volume: |
289 |
Pages: |
319-33 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wodara C |
Title: |
Cloning and characterization of sulfite dehydrogenase, two c-type cytochromes, and a flavoprotein of Paracoccus denitrificans GB17: essential role of sulfite dehydrogenase in lithotrophic sulfur oxidation. |
Year: |
1997 |
Journal: |
J Bacteriol |
Volume: |
179 |
Pages: |
5014-23 |
|
•
•
•
•
•
|
Publication |
First Author: |
Srivastava D |
Title: |
The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction. |
Year: |
2010 |
Journal: |
Biochemistry |
Volume: |
49 |
Pages: |
560-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Peralta DA |
Title: |
The E3 ubiquitin-ligase SEVEN IN ABSENTIA like 7 mono-ubiquitinates glyceraldehyde-3-phosphate dehydrogenase 1 isoform in vitro and is required for its nuclear localization in Arabidopsis thaliana. |
Year: |
2016 |
Journal: |
Int J Biochem Cell Biol |
Volume: |
70 |
Pages: |
48-56 |
|
•
•
•
•
•
|
Ontology Term |
Description: |
Protein which, if defective, causes glutaricaciduria (GA), a metabolic disorder characterized by the excretion of glutaric acid in the urine Type I GA is caused by the deficiency of glutaryl-CoA dehydrogenase, a mitochondrial enzyme involved in the metabolism of lysine, hydroxylysine and tryptophan. Type II GA differs from type I in that multiple acyl-CoA dehydrogenase deficiencies result in a large excretion not only of glutaric acid but also of lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids. GA II can result from a deficiency of any one of 3 mitochondrial molecules: the alpha and beta subunits of electron transfer flavoprotein and electron transfer flavoprotein-ubiquinone oxidoreductase |
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•
•
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Protein Domain |
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•
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•
•
•
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Protein Domain |
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•
|
Protein Domain |
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•
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•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Protein Domain |
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•
•
•
•
•
|
Publication |
First Author: |
Missihoun TD |
Title: |
Sequence and functional analyses of the aldehyde dehydrogenase 7B4 gene promoter in Arabidopsis thaliana and selected Brassicaceae: regulation patterns in response to wounding and osmotic stress. |
Year: |
2014 |
Journal: |
Planta |
Volume: |
239 |
Pages: |
1281-98 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lee K |
Title: |
The mitochondrial pentatricopeptide repeat protein PPR19 is involved in the stabilization of NADH dehydrogenase 1 transcripts and is crucial for mitochondrial function and Arabidopsis thaliana development. |
Year: |
2017 |
Journal: |
New Phytol |
Volume: |
215 |
Pages: |
202-216 |
|
•
•
•
•
•
|
Publication |
First Author: |
Heinzelmann E |
Title: |
An acyl-CoA dehydrogenase is involved in the formation of the Delta cis3 double bond in the acyl residue of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis. |
Year: |
2005 |
Journal: |
Microbiology (Reading) |
Volume: |
151 |
Pages: |
1963-1974 |
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
1 |
Description: |
Aldehyde dehydrogenase family 3 member H1 |
Type: |
chain |
End: |
484 |
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
36 |
Description: |
NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial |
Type: |
chain |
End: |
255 |
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
1 |
Description: |
NADH dehydrogenase [ubiquinone] iron-sulfur protein 5-A |
Type: |
chain |
End: |
118 |
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
1 |
Description: |
NADH dehydrogenase [ubiquinone] iron-sulfur protein 2 |
Type: |
chain |
End: |
394 |
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
1 |
Description: |
Aldehyde dehydrogenase family 2 member C4 |
Type: |
chain |
End: |
501 |
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
31 |
Description: |
NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial |
Type: |
chain |
End: |
486 |
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
17 |
Description: |
2-oxoisovalerate dehydrogenase subunit beta 2, mitochondrial |
Type: |
chain |
End: |
358 |
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
57 |
Description: |
2-oxoisovalerate dehydrogenase subunit alpha 1, mitochondrial |
Type: |
chain |
End: |
472 |
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
55 |
Description: |
Probable NAD(P)H dehydrogenase subunit CRR3, chloroplastic |
Type: |
chain |
End: |
174 |
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
1 |
Description: |
Probable NAD(P)H dehydrogenase (quinone) FQR1-like 2 |
Type: |
chain |
End: |
273 |
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
1 |
Description: |
Probable NAD(P)H dehydrogenase (quinone) FQR1-like 1 |
Type: |
chain |
End: |
205 |
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
1 |
Description: |
Aldehyde dehydrogenase family 3 member F1 |
Type: |
chain |
End: |
484 |
|
•
•
•
•
•
|
UniProt Feature |
|
Description: |
2-oxoisovalerate dehydrogenase subunit alpha 2, mitochondrial |
Type: |
chain |
End: |
472 |
|
•
•
•
•
•
|