ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P11295


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name IUCD_ECOLX
Primary accession number P11295
Secondary accession numbers O06897 O30770
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on December 15, 1998 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 62)
Name and origin of the protein
Protein name L-lysine 6-monooxygenase
Synonyms EC 1.14.13.59
Lysine 6-N-hydroxylase
Lysine N(6)-hydroxylase
Lysine-N-oxygenase
Gene name
Name: iucD
Synonyms: aerA
From
Escherichia coli [TaxID: 562] 
Encoded on Plasmid IncFI ColV3-K30; Plasmid ColV-K311.
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
PLASMID=IncFI ColV3-K30;
PubMed=3275632 [NCBI, ExPASy, EBI, Israel, Japan]
Herrero M., de Lorenzo V., Neilands J.B.;
"Nucleotide sequence of the iucD gene of the pColV-K30 aerobactin operon and topology of its product studied with phoA and lacZ gene fusions.";
J. Bacteriol. 170:56-64(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PLASMID=IncFI ColV3-K30;
Marrone L., Viswanatha T.;
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF PRO-14.
PLASMID=ColV-K311;
STRAIN=K-311;
DOI=10.1515/BC.1999.006; PubMed=10064136 [NCBI, ExPASy, EBI, Israel, Japan]
Stehr M., Smau L., Singh M., Seth O., Macheroux P., Ghisla S., Diekmann H.;
"Studies with lysine N6-hydroxylase. Effect of a mutation in the assumed FAD binding site on coenzyme affinities and on lysine hydroxylating activity.";
Biol. Chem. 380:47-54(1999).
Comments
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
M18968; AAA23196.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U90207; AAC00523.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF016586; AAB71391.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF016587; AAB71392.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28665; BVECID.
3D structure databases
ModBase P11295.
Enzyme and pathway databases
BioCyc MetaCyc:MON-11590; -.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0047091; Molecular function: L-lysine 6-monooxygenase (NADPH) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
BLOCKS P11295.
Other
ProtoNet P11295.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Ion transport; Iron; Iron transport; Membrane; NADP; Oxidoreductase; Plasmid; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   425  425     L-lysine 6-monooxygenase. PRO_0000204028
NP_BIND   8    14  7     FAD (Potential). 
MUTAGEN   14    14        P->G: Low activity. 
CONFLICT   139   139        E -> Q (in Ref. 1; AAA23196). 
CONFLICT   172   172        M -> S (in Ref. 1; AAA23196). 
CONFLICT   231   231        E -> D (in Ref. 1; AAA23196). 
CONFLICT   258   267        MTSDGITADS -> TDIGWHHCPIL (in Ref. 1; AAA23196). 
Sequence information
Length: 425 AA [This is the length of the unprocessed precursor] Molecular weight: 48726 Da [This is the MW of the unprocessed precursor] CRC64: 0F8B2A2F87E39751 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKKSVDFIGV GTGPFNLSIA ALSHQIEELD CLFFDEHPHF SWHPGMLVPD CHMQTVFLKD 

        70         80         90        100        110        120 
LVSAVAPTNP YSFVNYLVKH KKFYRFLTSR LRTVSREEFS DYLRWAAEDM NNLYFSHTVE 

       130        140        150        160        170        180 
NIDFDKKRRL FLVQTSQGEY FARNICLGTG KQPYLPPCVK HMTQSCFHAS EMNLRRPDLS 

       190        200        210        220        230        240 
GKRITVVGGG QSGADLFLNA LRGEWGEAAE INWVSRRNNF NALDEAAFAD EYFTPEYISG 

       250        260        270        280        290        300 
FSGLEEDIRH QLLDEQKMTS DGITADSLLT IYRELYHRFE VLRKPRNIRL LPSRSVTTLE 

       310        320        330        340        350        360 
SSGPGWKLLM EHHLDQGRES LESDVVIFAT GYRSALPQIL PSLMPLITMH DKNTFKVRDD 

       370        380        390        400        410        420 
FTLEWSGPKE NNIFVVNASM QTHGIAEPQL SLMAWRSARI LNRVMGRDLF DLSMPPALIQ 


WRSGT 

P11295 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

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

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!