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Annotation rule MF_02074 |
Accession | MF_02074 |
Dates | 30-AUG-2016 (Created) 19-NOV-2022 (Last updated, Version 6) |
Name | Bact_renalase |
Scope | Bacteria; Pseudomonadales |
Templates | Q48MT7 (RNLS_PSE14); Q888A4 (RNLS_PSESM): [Recover all] |
Triggered by |
Identifier |
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Protein name |
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Function | Catalyzes the oxidation of the 1,2-dihydro- and 1,6-dihydro- isomeric forms of beta-NAD(P) back to beta-NAD(P)+. May serve to protect primary metabolism dehydrogenases from inhibition by the 1,2-dihydro- and 1,6-dihydro-beta-NAD(P) isomers. |
Catalytic activity | RHEA:40395: 1,2-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+)
EC 1.6.3.5 |
RHEA:40399: 1,2-dihydro-beta-NADP + H(+) + O2 = H2O2 + NADP(+)
EC 1.6.3.5 |
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RHEA:48000: 1,6-dihydro-beta-NADP + H(+) + O2 = H2O2 + NADP(+)
EC 1.6.3.5 |
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RHEA:47996: 1,6-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+)
EC 1.6.3.5 |
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Cofactor | FAD |
Similarity | Belongs to the bacterial renalase family. |
Pfam | PF01593; Amino_oxidase; 1; |
From: RNLS_PSE14 (Q48MT7) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING (Optional) | 32 | 33 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692 | [DE]-K | ||||||||
BINDING (Optional) | 56 | 57 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692 | Q-Y | ||||||||
BINDING (Optional) | 57 | 61 | /ligand="substrate | Y-F-T-x-R | ||||||||
BINDING (Optional) | 96 | 98 | /ligand="substrate | S-P-D | ||||||||
BINDING (Optional) | 13 | 13 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692 | [AS] | ||||||||
BINDING (Optional) | 40 | 40 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692 | R | ||||||||
BINDING (Optional) | 128 | 128 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692 | [IV] | ||||||||
BINDING (Optional) | 185 | 185 | /ligand="substrate | T | ||||||||
BINDING (Optional) | 302 | 302 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692 | D | ||||||||
BINDING (Optional) | 308 | 308 | /ligand="substrate | R | ||||||||
BINDING (Optional) | 309 | 309 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692 | V |
Size range | 320-350 amino acids |
Related rules | None |
Fusion | None |