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UniProtKB/Swiss-Prot entry O85762


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SSUE_PSEPU
Primary accession number O85762
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on July 19, 2004 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 34)
Name and origin of the protein
Protein name FMN reductase
Synonym EC 1.5.1.29
Gene name
Name: ssuE
From
Pseudomonas putida [TaxID: 303] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=DSM 6884 / S-313;
DOI=10.1128/JB.182.10.2869-2878.2000; PubMed=10781557 [NCBI, ExPASy, EBI, Israel, Japan]
Kahnert A., Vermeij P., Wietek C., James P., Leisinger T., Kertesz M.A.;
"The ssu locus plays a key role in organosulfur metabolism in Pseudomonas putida S-313.";
J. Bacteriol. 182:2869-2878(2000).
[2]
SEQUENCE REVISION.
Kertesz M.A.;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
Comments
  • FUNCTION: Probably forms a two-component reduced flavin mononucleotide-dependent monooxygenase by binding to ssuD. Required for growth on aliphatic sulfonates or methionine but not arylsulfonates.
  • CATALYTIC ACTIVITY: FMNH2 + NAD(P)+ = FMN + NAD(P)H.
  • SIMILARITY: Belongs to the ssuE family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF075709; AAC31903.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase O85762.
Ontologies
GO
GO:0008752; Molecular function: FMN reductase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR005025; FMN_red.
Graphical view of domain structure.
Pfam PF03358; FMN_red; 1.
Pfam graphical view of domain structure.
BLOCKS O85762.
ProtoNet O85762.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
FMN; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   197  197     FMN reductase. PRO_0000160593
Sequence information
Length: 197 AA [This is the length of the unprocessed precursor] Molecular weight: 21459 Da [This is the MW of the unprocessed precursor] CRC64: 2244E3289528FDC2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLVVSIGGSP STRSRSGVLL ERSRQWLQDR GVEVVSFQVR DFPAEDLLHA RFDSPQVQHF 

        70         80         90        100        110        120 
QQLVAQADGL VVATPVYKAS FAGALKTLLD LLPERALEHK IVLPIATGGS IAHMLAVDYA 

       130        140        150        160        170        180 
LKPVLSALKA QETLQGIFAD DSQIAYGEGA KPAQLAPALE ERLHDSLETF HVALARRPRP 

       190 
VAPGVLNERL ISARWSI 

O85762 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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