| IED ID | IndEnz0010001432 |
| Enzyme Type ID | esterase001432 |
| Protein Name |
Rubredoxin-NAD + reductase RdxR EC 1.18.1.1 |
| Gene Name | rubB ACIAD1065 |
| Organism | Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Moraxellales Moraxellaceae Acinetobacter Acinetobacter baylyi Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) |
| Enzyme Sequence | MHPIVIIGSGMAGYTLAREFRKLNPEHELVMICADDAVNYAKPTLSNALSGNKAPEQIPLGDAEKMSTQLKLQILSETWVKAINPETHELKLEKNGQETIQPYSKLVLAVGANPTRLAIAGDGSDDIHVVNSLIDYRAFRENLAKRQDKRVVILGAGLIGCEFANDLQHTGHQVTVIDLSPRPLGRLLPAHIADAFQKNLEESGIHFVLSTTVEKVSKINDGQDYAVTLANGQTLVADIVLSAIGLQPNIDLAKHAGVHTSRGILTNSLLETNLEDIYAIGDCAEVNGTLLPYVMPIMQQARALAKTLSGETTHVHYPAMPVAVKTPAAPLTVLPVPVDVDVNWETEEFEDGMLAKAIDNTDTLRGFVLLGATAGKQRLTLTKLVPDLIPAQL |
| Enzyme Length | 393 |
| Uniprot Accession Number | P42454 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 42; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q9HTK9; BINDING 80; /note=FAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q9HTK9; BINDING 162; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q9HTK9; BINDING 282; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q9HTK9; BINDING 294; /note=FAD; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q9HTK9; BINDING 325; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q9HTK9 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H(+) + NAD(+) + 2 reduced [rubredoxin] = NADH + 2 oxidized [rubredoxin]; Xref=Rhea:RHEA:18597, Rhea:RHEA-COMP:10302, Rhea:RHEA-COMP:10303, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.18.1.1; |
| DNA Binding | |
| EC Number | 1.18.1.1 |
| Enzyme Function | FUNCTION: Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase. {ECO:0000269|PubMed:10400587}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Hydrocarbon metabolism; alkane degradation. |
| nucleotide Binding | NP_BIND 9..12; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q9HTK9; NP_BIND 33..34; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q9HTK9 |
| Features | Binding site (6); Chain (1); Nucleotide binding (2); Sequence conflict (2) |
| Keywords | Cytoplasm;FAD;Flavoprotein;NAD;Oxidoreductase;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:10400587}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,464 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:18597 |
| Cross Reference Brenda |