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Reviewed, UniProtKB/Swiss-Prot P84469 (FERB_PARDE)

Last modified January 20, 2009. Version 18. 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:
    Ferric reductase B
    EC=1.16.1.7
Gene names
Name: ferB
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length27 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Reductase activity that acts on Fe3+-chelates and uses both NADH and NADPH as electron donors. May play a role in iron uptake. Ref.1

Catalytic activity

2 Fe2+ + NAD+ = 2 Fe3+ + NADH. Ref.1

Cofactor

Binds 1 FAD per subunit. Ref.1

Subunit structure

Homodimer. Ref.1

Induction

By Fe3+ ion deprivation. Ref.1

biophysicochemical properties

Kinetic parameters:

KM=0.4 mM for Fe3+EGTA and NADH

KM=1.6 mM for Fe3+EDTA and NADH

KM=0.4 mM for Fe3+citrate and NADH

KM=0.4 mM for Fe3+chloride and NADH

Mass spectrometry

Molecular mass is 20196 Da from positions 1 - ?. Determined by MALDI. Ref.1

Ontologies

Keywords
   Biological processElectron transport
Transport
   LigandFAD
Flavoprotein
NAD
NADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionferric-chelate reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›27›27Ferric reductase B
PRO_0000087228

Experimental info

Non-terminal residue271

Sequences

Sequence LengthMass (Da)Tools
P84469-1 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: 10D878742BCD3F4B

FASTA273,012
        10         20 
MVKTVAVMVG SLRKDSLAHK LMKVLQK 

« Hide

References

[1]"Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans."
Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.
Eur. J. Biochem. 271:553-562(2004) [PubMed: 14728682] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MASS SPECTROMETRY.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.16.1.7. 59.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameFERB_PARDE
AccessionPrimary (citable) accession number: P84469
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: January 20, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information