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0NCB5R_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCYB5R3
DescriptionNadh-cytochrome b5 reductase (ec 1.6.2.2) (b5r) (diaphorase-1) (cytochrome b5 reductase 3) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (TAS)
0005833 hemoglobin complex (TAS)
0016020 membrane (TAS)
0004128 cytochrome-b5 reductase activity (TAS)
0008015 circulation (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
These sequences contain an oxidoreductase FAD-binding domain. To date.he 3D-structures of the flavoprotein domain of Zea mays nitrate reductase and of pig NADH:cytochrome b5 reductase have been solved. The overall fold is similar to that of ferredoxin:NADP+ reductase : the FAD-binding domain (N-terminal) has the topology of an anti-parallel beta-barrel.hile the NAD(P)-binding domain (C-terminal) has the topology of a classical pyridine dinucleotide-binding fold (i.e. a central parallel beta-sheet flanked by 2 helices on each side).
  IPR008333:Oxidoreductase FAD-binding region
Bacterial ferredoxin-NADP+ reductase may be bound to the thylakoid membrane or anchored to the thylakoid-bound phycobilisomes.Chloroplast ferredoxin-NADP+ reductase () may play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. It is involved in the final step in the linear photosynthetic electron transport chain and has also been implicated in cyclic electron flow around photosystem I where its role would be to return electrons from ferredoxin to the cytochrome B-F complex.This domain is present in a variety of proteins that include.acterial flavohemoprotein.ammalian NADH-cytochrome b5 reductase.ukaryotic NADPH-cytochrome P450 reductase.itrate reductase from plants.itric-oxide synthase.acterial vanillate demethylase and others.
  IPR001433:Oxidoreductase FAD/NAD(P)-binding
Flavoprotein pyridine nucleotide cytochrome reductases (FPNCR) catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes include ferredoxin:NADP+reductases (FNR) .lant and fungal NAD(P)H:nitrate reductases NADH:cytochrome b5 reductases .ADPH:P450 reductases .ADPH:sulphite reductases .itric oxide synthases .hthalate dioxygenase reductase .nd various other flavoproteins.Despite functional similarities.PNCRs show no sequence similarity to NADPH:adrenodoxin reductases .or to bacterial ferredoxin:NAD+reductases and their homologues . To date.D-structures of 4 members of the family have been solved: Spinacia oleracea (spinach) ferredoxin:NADP+ reductase ; Pseudomonas cepacia phthalate dioxygenase reductase ; the flavoprotein domain of Zea mays (corn) nitrate reductase ; and Sus scrofa (pig) NADH:cytochrome b5 reductase . In all of them.he FAD-binding domain (N-terminal) has the topology of an anti-parallel beta-barrel.hile the NAD(P)-binding domain (C-terminal) has the topology of a classical pyridine dinucleotide-binding fold (i.e. a central parallel beta-sheet with 2 helices on each side) . In spite of such structural similarities.he level of amino acid identity between family members is at or below the limit of significance (e.g..itrate reductase is only 15% identical to FNR) .
  IPR001709:Flavoprotein pyridine nucleotide cytochrome reductase
Flavoprotein pyridine nucleotide cytochrome reductases (FPNCR) catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes includeferredoxin:NADP+ reductases (FNR) .plant and fungal NAD(P)H:nitrate reductases .NADH:cytochrome b5 reductases .NADPH:P450 reductases.NADPH:sulphite reductases.nitric oxide synthases.phthalate dioxygenase reductase.and various other flavoproteins.NADH:cytochrome b5 reductase (CBR) serves as electron donor for cytochrome b5. ubiquitous electron carrier (see ).hus participating in a variety of metabolic pathways (including steroid biosynthesis.esaturation and elongation of fatty acids.450-dependent reactions.ethaemoglobin reduction.tc.). A membrane-bound form of CBR is located on the cytosolic side of the endoplasmic reticulum.hile a soluble form is found in erythrocytes . In the membrane-bound form.he N-terminal residue is myristoylated . Deficiency of the erythrocyte form causes hereditary methaemoglobinemia .In biological nitrate assimilation.eduction of nitrate to nitrite is catalysed by the multidomain redox enzyme NAD(P)H:nitrate reductase (NR). Three forms of NR are known: an NADH-specific enzyme found in higher plants and algae (); an NAD(P)H-bispecific enzyme found in higher plants.lgae and fungi (); and an NADPH-specific enzyme found only in fungi () . NR can be divided into 3 structure/function domains: the molybdopterin cofactor binds in the N-terminal domain; the central region is the cytochrome b domain.hich is similar to animal cytochrome b5 (see ); and the C-terminal portion of the protein is occupied by the FAD/NAD(P)H binding domain.hich is similar to CBR . The catalytic reduction of nitrate to nitrite can be viewed as a single polypeptide electron transport chain with electron flow from NAD(P)H -> FAD -> cytochrome b5 -> molybdopterin -> NO(3). Thus.he flavin domain of NR is functionally identical to CBR.To date.he 3D-structures of the flavoprotein domain of Zea mays nitrate reductase and of pig NADH:cytochrome b5 reductase have been solved. The overall fold is similar to that of ferredoxin:NADP+ reductase : the FAD-binding domain (N-terminal) has the topology of an anti-parallel beta-barrel.hile the NAD(P)-binding domain (C-terminal) has the topology of a classical pyridine dinucleotide-binding fold (i.e. a central parallel beta-sheet flanked by 2 helices on each side).
  IPR001834:NADH:cytochrome b5 reductase (CBR)
Flavoprotein pyridine nucleotide cytochrome reductases (FPNCR) catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes includeferredoxin:NADP+ reductases (FNR) .plant and fungal NAD(P)H:nitrate reductases .NADH:cytochrome b5 reductases .NADPH:P450 reductases.NADPH:sulphite reductases.nitric oxide synthases.phthalate dioxygenase reductase.and various other flavoproteins.Cytochrome b5 reductase (CBR) serves as electron donor for cytochrome b5. ubiquitous electron carrier (see ).hus participating in a variety of metabolic pathways.NADH + H+ + 2 ferricytochrome b5 = NAD+ + 2 ferrocytochrome b5CBR exists in two isoforms produced by the use of alternative promoters. The membrane-bound isoform is located on the cytosolic side of the endoplasmic reticulum and mitochondrial outer membrane and participates in a variety of metabolic transformations.ncluding steroid biosynthesis.esaturation and elongation of fatty acids.nd P450-dependent reactions. The N-terminal residue of this form is myristoylated . The soluble isoform is found in erythrocytes and is involved in the electron-transport system for reducing methaemoglobin to functional haemoglobin . Deficiency of the erythrocyte form causes hereditary methaemoglobinemia .The soluble form of CBR consists of two domains.n N-terminal FAD-binding domain.nd a C-terminal NADH-binding domain . The FAD-binding domain has an antiparallel beta-barrel topology.hile the NAD-binding domain forms the three-layered alpha-beta-alpha fold typical of pyridine dinucleotide-binding regions. In a mutant form of CBR that causes methaemoglobinemia.he adenosine diphosphate (ADP) moiety of the FAD prosthetic group is displaced into the corresponding ADP binding site of the physiological substrate.ADH.hus acting as a substrate inhibitor and severely reducing enzyme activity .
  IPR012260:Cytochrome-b5 reductase
IPR008333:FAD_binding_6 
Evalue:-63.6575775146484 
Location:43-150IPR001433:NAD_binding_1 
Evalue:-44.7695503234863 
Location:175-284
SequencesProtein: NCB5R_HUMAN (300 aa)
mRNA: NM_000398
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK00326
  Level 3 annotation:
    cytochrome-b5 reductase
  Level 2 annotation:
    Aminosugars metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 378 residues, 41344764-41345895Exon2: 35 residues, 41349738-41349838Exon3: 30 residues, 41353253-41353339Exon4: 30 residues, 41353554-41353638Exon5: 45 residues, 41354101-41354231Exon6: 37 residues, 41356831-41356938Exon7: 26 residues, 41357327-41357400Exon8: 46 residues, 41362664-41362796Exon9: 37 residues, 41375244-41375349Exon10: 2 residues, -Jump to NCB5R_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4575 41595721-41741095 ~-145K 24901(PACSIN2)(-)Loci: 4576 41765589-41815373 ~-50K 24903(TTLL1)(-)Loci: 3322 41877478-41889191 ~-12K 24908(BZRP)(+)Loci: 4574 41344764-41375349 ~-31K 24894(CYB5R3)(-)Link out to UCSC