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Reviewed, UniProtKB/Swiss-Prot P84468 (FERA_PARDE)

Last modified January 20, 2009. Version 13. 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 A
    EC=1.16.1.7
Gene names
Name: ferA
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length20 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 NADH as an electron donor and requires the presence of FMN for full activity. May play a role in iron uptake. Ref.1

Catalytic activity

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

Subunit structure

Monomer. Ref.1

Induction

By Fe3+ ion deprivation. Ref.1

Mass spectrometry

Molecular mass is 18814 Da from positions 1 - ?. Determined by MALDI. It is not clear why there are 2 peaks for this protein. Ref.1

Molecular mass is 18917 Da from positions 1 - ?. Determined by MALDI. Ref.1

Ontologies

Keywords
   Biological processElectron transport
Transport
   LigandFMN
Flavoprotein
NAD
   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 – ›20›20Ferric reductase A
PRO_0000087227

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P84468-1 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: F9884FCE24EA0F5A

FASTA202,246
        10         20 
SRLPPATRDK LADEITFFPA 

« 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, 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 nameFERA_PARDE
AccessionPrimary (citable) accession number: P84468
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: January 20, 2009
This is version 13 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