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Search results 4701 to 4800 out of 5170 for xanthine dehydrogenase

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Type Details Score
UniProt Feature
UniProt Feature
Begin: 107
Description: Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding
Type: domain
End: 258
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UniProt Feature
UniProt Feature
Begin: 6
Description: Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding
Type: domain
End: 156
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UniProt Feature
UniProt Feature
Begin: 328
Description: Shikimate dehydrogenase substrate binding N-terminal
Type: domain
End: 408
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UniProt Feature
UniProt Feature
Begin: 79
Description: Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding
Type: domain
End: 228
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UniProt Feature
UniProt Feature
Begin: 82
Description: Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding
Type: domain
End: 235
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UniProt Feature
UniProt Feature
Begin: 87
Description: Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding
Type: domain
End: 236
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UniProt Feature
UniProt Feature
Begin: 283
Description: Shikimate dehydrogenase substrate binding N-terminal
Type: domain
End: 363
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UniProt Feature
UniProt Feature
Begin: 1
Description: Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding
Type: domain
End: 109
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UniProt Feature
UniProt Feature
Begin: 55
Description: Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding
Type: domain
End: 206
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UniProt Feature
UniProt Feature
Begin: 511
Description: NADH dehydrogenase subunit 5 C-terminal
Type: domain
End: 638
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UniProt Feature
UniProt Feature
Begin: 71
Description: Cytokinin dehydrogenase 1 FAD/cytokinin binding
Type: domain
End: 344
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UniProt Feature
UniProt Feature
Begin: 161
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 339
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UniProt Feature
UniProt Feature
Begin: 87
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 354
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UniProt Feature
UniProt Feature
Begin: 112
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 162
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UniProt Feature
UniProt Feature
Begin: 60
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 144
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UniProt Feature
UniProt Feature
Begin: 6
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 110
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UniProt Feature
UniProt Feature
Begin: 121
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 295
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UniProt Feature
UniProt Feature
Begin: 52
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 326
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UniProt Feature
UniProt Feature
Begin: 58
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 325
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UniProt Feature
UniProt Feature
Begin: 132
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 310
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UniProt Feature
UniProt Feature
Begin: 37
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 304
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UniProt Feature
UniProt Feature
Begin: 100
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 273
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UniProt Feature
UniProt Feature
Begin: 84
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 150
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UniProt Feature
UniProt Feature
Begin: 158
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 263
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UniProt Feature
UniProt Feature
Begin: 119
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 224
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UniProt Feature
UniProt Feature
Begin: 45
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 111
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UniProt Feature
UniProt Feature
Begin: 119
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 238
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UniProt Feature
UniProt Feature
Begin: 45
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 242
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UniProt Feature
UniProt Feature
Begin: 116
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 289
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UniProt Feature
UniProt Feature
Begin: 35
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 320
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UniProt Feature
UniProt Feature
Begin: 52
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 325
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UniProt Feature
UniProt Feature
Begin: 121
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 294
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UniProt Feature
UniProt Feature
Begin: 24
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 134
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UniProt Feature
UniProt Feature
Begin: 36
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 320
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UniProt Feature
UniProt Feature
Begin: 116
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 289
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UniProt Feature
UniProt Feature
Begin: 87
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 354
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UniProt Feature
UniProt Feature
Begin: 161
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 339
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UniProt Feature
UniProt Feature
Begin: 132
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 305
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UniProt Feature
UniProt Feature
Begin: 65
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 336
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UniProt Feature
UniProt Feature
Begin: 112
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 162
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UniProt Feature
UniProt Feature
Begin: 35
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 320
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UniProt Feature
UniProt Feature
Begin: 116
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 289
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UniProt Feature
UniProt Feature
Begin: 124
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 306
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UniProt Feature
UniProt Feature
Begin: 130
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 322
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UniProt Feature
UniProt Feature
Begin: 29
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 346
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UniProt Feature
UniProt Feature
Begin: 132
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 306
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UniProt Feature
UniProt Feature
Begin: 65
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 337
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UniProt Feature
UniProt Feature
Begin: 112
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 162
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UniProt Feature
UniProt Feature
Begin: 115
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 297
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UniProt Feature
UniProt Feature
Begin: 273
Description: D-isomer specific 2-hydroxyacid dehydrogenase catalytic
Type: domain
End: 590
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UniProt Feature
UniProt Feature
Begin: 374
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 566
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UniProt Feature
UniProt Feature
Begin: 3
Description: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Type: domain
End: 179
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UniProt Feature
UniProt Feature
Begin: 46
Description: Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding
Type: domain
End: 134
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UniProt Feature
UniProt Feature
Begin: 6
Description: Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding
Type: domain
End: 148
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Protein Domain
IPR012027
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Protein Domain
IPR016099
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Protein Domain
IPR002376
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Protein Domain
IPR029035
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Protein Domain
IPR033888
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Protein Domain
IPR022291
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Protein Domain
IPR044304
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Protein Domain
IPR019478
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Protein Domain
IPR003420
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Protein Domain
IPR003680
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Protein Domain
IPR037115
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Protein Domain
IPR048068
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Protein Domain
IPR000415
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Protein Domain
IPR011254
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Protein Domain
IPR008030
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Protein Domain
IPR006115
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Protein Domain
IPR006114
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Publication
8972600
First Author: Park SC
Title: Cis-acting elements essential for light regulation of the nuclear gene encoding the A subunit of chloroplast glyceraldehyde 3-phosphate dehydrogenase in Arabidopsis thaliana.
Year: 1996
Journal: Plant Physiol
Volume: 112
Pages: 1563-71
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Publication
24096342
First Author: Armbruster U
Title: The photosynthesis affected mutant68-like protein evolved from a PSII assembly factor to mediate assembly of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis.
Year: 2013
Journal: Plant Cell
Volume: 25
Pages: 3926-43
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Publication
12047629
First Author: Gatzek S
Title: Antisense suppression of l-galactose dehydrogenase in Arabidopsis thaliana provides evidence for its role in ascorbate synthesis and reveals light modulated l-galactose synthesis.
Year: 2002
Journal: Plant J
Volume: 30
Pages: 541-53
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Publication
19087955
First Author: Saballos A
Title: A genomewide analysis of the cinnamyl alcohol dehydrogenase family in sorghum [Sorghum bicolor (L.) Moench] identifies SbCAD2 as the brown midrib6 gene.
Year: 2009
Journal: Genetics
Volume: 181
Pages: 783-95
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Publication
22195593
First Author: Wallström SV
Title: An alternatively spliced domain of the NDC1 NAD(P)H dehydrogenase gene strongly influences the expression of the ACTIN2 reference gene in Arabidopsis thaliana.
Year: 2012
Journal: Plant Sci
Volume: 183
Pages: 190-6
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Publication
23054470
First Author: Fontaine JX
Title: Characterization of a NADH-dependent glutamate dehydrogenase mutant of Arabidopsis demonstrates the key role of this enzyme in root carbon and nitrogen metabolism.
Year: 2012
Journal: Plant Cell
Volume: 24
Pages: 4044-65
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Publication
11917081
First Author: Fujiki Y
Title: Activation of the promoters of Arabidopsis genes for the branched-chain alpha-keto acid dehydrogenase complex in transgenic tobacco BY-2 cells under sugar starvation.
Year: 2002
Journal: Plant Cell Physiol
Volume: 43
Pages: 275-80
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Publication
8061040
First Author: Luethy MH
Title: The nucleotide and deduced amino acid sequences of a cDNA encoding the E1 beta-subunit of the Arabidopsis thaliana mitochondrial pyruvate dehydrogenase complex.
Year: 1994
Journal: Biochim Biophys Acta
Volume: 1187
Pages: 95-8
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Publication
23036115
First Author: Huang S
Title: Succinate dehydrogenase assembly factor 2 is needed for assembly and activity of mitochondrial complex II and for normal root elongation in Arabidopsis.
Year: 2013
Journal: Plant J
Volume: 73
Pages: 429-41
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Publication
10486141
First Author: Maklashina E
Title: Comparison of catalytic activity and inhibitors of quinone reactions of succinate dehydrogenase (Succinate-ubiquinone oxidoreductase) and fumarate reductase (Menaquinol-fumarate oxidoreductase) from Escherichia coli.
Year: 1999
Journal: Arch Biochem Biophys
Volume: 369
Pages: 223-32
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Publication
11796730
First Author: Dobritzsch D
Title: Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer.
Year: 2002
Journal: J Biol Chem
Volume: 277
Pages: 13155-66
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Publication
9352901
First Author: Yum DY
Title: Cloning and expression of a gene cluster encoding three subunits of membrane-bound gluconate dehydrogenase from Erwinia cypripedii ATCC 29267 in Escherichia coli.
Year: 1997
Journal: J Bacteriol
Volume: 179
Pages: 6566-72
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Publication
9920875
First Author: Igarashi K
Title: Cellobiose dehydrogenase from the fungi Phanerochaete chrysosporium and Humicola insolens. A flavohemoprotein from Humicola insolens contains 6-hydroxy-FAD as the dominant active cofactor.
Year: 1999
Journal: J Biol Chem
Volume: 274
Pages: 3338-44
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Publication
17222187
First Author: Sundaramoorthy R
Title: Crystal structures of a bacterial 6-phosphogluconate dehydrogenase reveal aspects of specificity, mechanism and mode of inhibition by analogues of high-energy reaction intermediates.
Year: 2007
Journal: FEBS J
Volume: 274
Pages: 275-86
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Publication
8308022
First Author: LéJohn HB
Title: Molecular characterization of an NAD-specific glutamate dehydrogenase gene inducible by L-glutamine. Antisense gene pair arrangement with L-glutamine-inducible heat shock 70-like protein gene.
Year: 1994
Journal: J Biol Chem
Volume: 269
Pages: 4523-31
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Publication
8389187
First Author: Matsushita K
Title: A novel quinoprotein methanol dehydrogenase containing an additional 32-kilodalton peptide purified from Acetobacter methanolicus: identification of the peptide as a MoxJ product.
Year: 1993
Journal: Biochemistry
Volume: 32
Pages: 5576-82
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Publication
24449431
First Author: García-Cazorla A
Title: Two novel mutations in the BCKDK (branched-chain keto-acid dehydrogenase kinase) gene are responsible for a neurobehavioral deficit in two pediatric unrelated patients.
Year: 2014
Journal: Hum Mutat
Volume: 35
Pages: 470-7
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Publication
7009604
First Author: Thomson JW
Title: The respiratory chain NADH dehydrogenase of Escherichia coli. Isolation of an NADH:quinone oxidoreductase from membranes and comparison with the membrane-bound NADH:dichlorophenolindophenol oxidoreductase.
Year: 1981
Journal: J Biol Chem
Volume: 256
Pages: 3077-84
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Publication
26063505
First Author: Clark TJ
Title: Analysis of Loss-of-Function Mutants in Aspartate Kinase and Homoserine Dehydrogenase Genes Points to Complexity in the Regulation of Aspartate-Derived Amino Acid Contents.
Year: 2015
Journal: Plant Physiol
Volume: 168
Pages: 1512-26
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Protein Domain
IPR005719
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Protein Domain
IPR001653
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GO Term
GO:0047103 | 3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-oxidoreductase activity
Description: Catalysis of the reaction: H2O + NAD+ + 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-al = NADH + 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate.
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GO Term
GO:0042652 | mitochondrial respiratory chain complex I, peripheral segment
Description: The peripheral segment of respiratory chain complex I located in the mitochondrion. Respiratory chain complex I is an enzyme of the respiratory chain, consisting of at least 34 polypeptide chains. The electrons of NADH enter the chain at this complex. The complete complex is L-shaped, with a horizontal arm lying in the membrane and a vertical arm that projects into the matrix.
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GO Term
GO:0050166 | pantoate 4-dehydrogenase activity
Description: Catalysis of the reaction: (R)-pantoate + NAD+ = (R)-4-dehydropantoate + H+ + NADH.
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GO Term
GO:0052874 | FMN reductase (NADH) activity
Description: Catalysis of the reaction: FMNH2 + NAD+ = FMN + NADH + 2 H+.
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Protein Domain
IPR010266
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Protein Domain
IPR015405
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Protein Domain
IPR039944
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Protein Domain
IPR023885
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