IED ID | IndEnz0018001578 |
Enzyme Type ID | peroxidase001578 |
Protein Name |
NADH--cytochrome b5 reductase 1 EC 1.6.2.2 |
Gene Name | CBR1 CBR At5g17770 MVA3.13 |
Organism | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
Enzyme Sequence | MDTEFLRTLDRQILLGVFVAFVAVGAGAAYFLTSSKKRRVCLDPENFKEFKLVKRHQLSHNVAKFVFELPTSTSVLGLPIGQHISCRGKDGQGEDVIKPYTPTTLDSDVGRFELVIKMYPQGRMSHHFREMRVGDHLAVKGPKGRFKYQPGQFRAFGMLAGGSGITPMFQVARAILENPTDKTKVHLIYANVTYDDILLKEELEGLTTNYPEQFKIFYVLNQPPEVWDGGVGFVSKEMIQTHCPAPASDIQILRCGPPPMNKAMAANLEALGYSPEMQFQF |
Enzyme Length | 281 |
Uniprot Accession Number | Q9ZNT1 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2; Evidence={ECO:0000269|PubMed:17227547, ECO:0000269|PubMed:9880378};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46681; Evidence={ECO:0000269|PubMed:17227547, ECO:0000269|PubMed:9880378}; |
DNA Binding | |
EC Number | 1.6.2.2 |
Enzyme Function | FUNCTION: Reductase transferring electrons from NADH to cytochrome b5. Required for the NADH-dependent electron transfer involved in the desaturation and hydroxylation of fatty acids and in the desaturation of sterol precursors. No activity with NADPH as electron donor. {ECO:0000269|PubMed:17227547, ECO:0000269|PubMed:9880378}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | NP_BIND 129..144; /note=FAD; /evidence=ECO:0000250; NP_BIND 155..187; /note=FAD; /evidence=ECO:0000250 |
Features | Chain (1); Domain (1); Frameshift (1); Modified residue (1); Motif (1); Mutagenesis (1); Nucleotide binding (2); Transmembrane (1) |
Keywords | FAD;Flavoprotein;Membrane;Mitochondrion;Mitochondrion outer membrane;NAD;Oxidoreductase;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:21896887}; Single-pass membrane protein {ECO:0000269|PubMed:21896887}. |
Modified Residue | MOD_RES 166; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P83291 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 15295017; 15596101; 16287169; 16618929; 17317660; 18775970; 20687615; 23995085; 25896488; 26712506; 27200011; |
Motif | MOTIF 34..40; /note=AKR2A-binding sequence (ABS) required for mitochondrion outer membrane targeting; /evidence=ECO:0000269|PubMed:21057222 |
Gene Encoded By | |
Mass | 31,490 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 uM for NADH {ECO:0000269|PubMed:9880378}; |
Metal Binding | |
Rhea ID | RHEA:46680; RHEA:46681 |
Cross Reference Brenda |