| IED ID | IndEnz0018000952 |
| Enzyme Type ID | peroxidase000952 |
| Protein Name |
Transmembrane ascorbate-dependent reductase CYB561 EC 7.2.1.- Chromomembrin B Cytochrome b-561 Cytochrome b561 |
| Gene Name | CYB561 |
| Organism | Bos taurus (Bovine) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MEGPASPARAPGALPYYVAFSQLLGLIVVAMTGAWLGMYRGGIAWESALQFNVHPLCMIIGLVFLQGDALLVYRVFRNEAKRTTKVLHGLLHVFAFVIALVGLVAVFEHHRKKGYADLYSLHSWCGILVFALFFAQWLVGFSFFLFPGASFSLRSRYRPQHVFFGAAIFLLSVATALLGLKEALLFELGTKYSMFEPEGVLANVLGLLLATFATVILYILTRADWKRPLQAEEQALSMDFKTLTEGDSPSSQ |
| Enzyme Length | 252 |
| Uniprot Accession Number | P10897 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 74; /note=Heme b 2; /evidence=ECO:0000250|UniProtKB:Q53TN4; BINDING 81; /note=Ascorbate; /evidence=ECO:0000250|UniProtKB:Q53TN4; BINDING 81; /note=Heme b 2; /evidence=ECO:0000250|UniProtKB:Q53TN4; BINDING 85; /note=Ascorbate; /evidence=ECO:0000250|UniProtKB:Q53TN4; BINDING 154; /note=Ascorbate; /evidence=ECO:0000250|UniProtKB:Q53TN4; BINDING 182; /note=Heme b 1; /evidence=ECO:0000250|UniProtKB:Q53TN4; BINDING 226; /note=Heme b 2; /evidence=ECO:0000250|UniProtKB:Q53TN4 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=L-ascorbate(in) + monodehydro-L-ascorbate radical(out) = L-ascorbate(out) + monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:66524, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; Evidence={ECO:0000269|PubMed:1623014, ECO:0000269|PubMed:18501187, ECO:0000269|PubMed:3597367};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66525; Evidence={ECO:0000305|PubMed:1623014}; |
| DNA Binding | |
| EC Number | 7.2.1.- |
| Enzyme Function | FUNCTION: Transmembrane reductase that uses ascorbate as an electron donor in the cytoplasm and transfers electrons across membranes to reduce monodehydro-L-ascorbate radical in the lumen of secretory vesicles (PubMed:3597367, PubMed:1623014, PubMed:18501187). It is therefore involved the regeneration and homeostasis within secretory vesicles of ascorbate which in turn provides reducing equivalents needed to support the activity of intravesicular enzymes (Probable). {ECO:0000269|PubMed:1623014, ECO:0000269|PubMed:18501187, ECO:0000269|PubMed:3597367, ECO:0000305|PubMed:3597367}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (7); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (4); Modified residue (3); Mutagenesis (12); Region (1); Topological domain (7); Transmembrane (6) |
| Keywords | Acetylation;Cytoplasmic vesicle;Direct protein sequencing;Electron transport;Heme;Iron;Membrane;Metal-binding;Phosphoprotein;Reference proteome;Translocase;Transmembrane;Transmembrane helix;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000269|PubMed:2460342}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. Note=Secretory vesicle containing catecholamines and amidated peptides. {ECO:0000269|PubMed:2460342}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000269|PubMed:12768340; MOD_RES 248; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q60720; MOD_RES 250; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q60720 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,904 |
| Kinetics | |
| Metal Binding | METAL 54; /note=Iron 1 (heme b 1 axial ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q53TN4; METAL 88; /note=Iron 2 (heme b 2 axial ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q53TN4; METAL 122; /note=Iron 1 (heme b 1 axial ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q53TN4; METAL 161; /note=Iron 2 (heme b 2 axial ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q53TN4 |
| Rhea ID | RHEA:66524; RHEA:66525 |
| Cross Reference Brenda | 7.2.1.3; |