[1]	PROTEIN SEQUENCE. TISSUE=Erythrocyte; PubMed=2172227 [NCBI, ExPASy, EBI, Israel, Japan] Abe Y., Ito T., Okazaki T.; "Purification and characterization of NADPH-dependent methemoglobin reductase from the nucleated erythrocytes of bullfrog, Rana catesbeiana."; J. Biochem. 108:255-260(1990).

Comments

FUNCTION: Catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. Possible role in protecting cells from oxidative damage or in regulating iron metabolism (By similarity).
CATALYTIC ACTIVITY: NADPH + acceptor = NADP⁺ + reduced acceptor.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 5.0 for NADPH-methemoglobin reductase activity, and 6.5 for NADPH-diaphorase activity;
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Potential).

Copyright

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Cross-references

Sequence databases

PX0038; PX0038.

3D structure databases

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0003959;	Molecular function: NADPH dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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Phylogenomic databases

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase.

Features

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Sequence information

Length: 24 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 2417 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 7B6CD31436FAC4EC [This is a checksum on the sequence]

        10         20 
APKNIVLFGA TGMTGQVTLG QALE

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools