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Reviewed, UniProtKB/Swiss-Prot P55736 (BLVRB_RANCA)

Last modified June 16, 2009. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesRecommended name:
    Flavin reductase
    EC=1.6.99.1
Alternative name(s):
    NADPH-dependent diaphorase
    NADPH-methemoglobin reductase
    NADPH-dehydrogenase
OrganismRana catesbeiana (Bull frog)
Taxonomic identifier8400 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

Protein attributes

Sequence length24 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm Potential.

biophysicochemical properties

pH dependence:

Optimum pH is 5.0 for NADPH-methemoglobin reductase activity, and 6.5 for NADPH-diaphorase activity.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADPH dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›24›24Flavin reductase
PRO_0000064950

Experimental info

Non-terminal residue241

Sequences

Sequence LengthMass (Da)Tools
P55736-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 7B6CD31436FAC4EC

FASTA242,417
        10         20 
APKNIVLFGA TGMTGQVTLG QALE 

« Hide

References

[1]"Purification and characterization of NADPH-dependent methemoglobin reductase from the nucleated erythrocytes of bullfrog, Rana catesbeiana."
Abe Y., Ito T., Okazaki T.
J. Biochem. 108:255-260(1990) [PubMed: 2172227] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Erythrocyte.

Cross-references

Sequence databases

PIRPX0038.

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENP55736.

Enzyme and pathway databases

BRENDA1.6.99.1. 829.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameBLVRB_RANCA
AccessionPrimary (citable) accession number: P55736
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information