Figure 3: The multiple amino acid sequence alignment of the MDHAR homologues and iron-sulphur protein reductases. | Scientific Reports

Figure 3: The multiple amino acid sequence alignment of the MDHAR homologues and iron-sulphur protein reductases.

From: Structure and catalytic mechanism of monodehydroascorbate reductase, MDHAR, from Oryza sativa L. japonica

Figure 3

Secondary structure elements of OsMDHAR are labelled above the sequence. The catalytic Tyr residue that mediates electron transfer is highlighted by a cyan box and arrow. The residues comprising the unique long loop are also highlighted by blue boxes. The residues that participate in the FAD and NAD binding are indicated by orange triangles pointing up and blue triangles pointing down, respectively. The Arg320 residue forming hydrogen bonds with bound AsA is highlighted by a magenta box and triangle pointing up. Accession data for amino acid sequences are as follows: OsMDHAR from O. sativa japonica (UniProtKB code Q9XFZ3); AtMDHAR from Arabidopsis thaliana (UniProtKB code Q9LFA3); ZmMDHAR from Zea mays (UniProtKB code B8A028); VvMDHAR, from Vitis vinifera (UniProtKB code A5JPK7); MdMDHAR from Malus domestica (UniProtKB code C0LQ98); GmMDHAR from Glycine max (UniProtKB code A0A0R0I177); BrMDHAR from Brassica rapa (UniProtKB code Q93 × 74); Pdr, putidaredoxin reductase from Pseudomonas putida (UniProtKB code M5AXR7); BphA4, ferredoxin reductase from Pseudomonas sp. (UniProtKB code Q52437); RdxR, rubredoxin reductase from P. aeruginosa (UniProtKB code A0A0E1B6R8).

Back to article page