Reviewed, UniProtKB/Swiss-Prot P11295 (IUCD_ECOLX)

Names and origin

Protein names

Recommended name:
    L-lysine 6-monooxygenase
    EC=1.14.13.59
Alternative name(s):
    Lysine 6-N-hydroxylase
    Lysine N(6)-hydroxylase
    Lysine-N-oxygenase

Gene names

Name:	iucD
Synonyms:	aerA

Encoded on

Plasmid IncFI ColV3-K30 Ref.1 Ref.2
Plasmid ColV-K311 Ref.3

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is one of the proteins involved in the biosynthesis of siderophores (such as the dihydroxamate siderophore, aerobactin), which are chelators that mediate the high-affinity iron transport systems induced by the organism under iron-stressed conditions.
Catalytic activity	L-lysine + NADPH + O2 = N(6)-hydroxy-L-lysine + NADP+ + H2O.
Cofactor	FAD By similarity.
Pathway	Siderophore biosynthesis; aerobactin biosynthesis.
Subcellular location	Cytoplasm. Cell membrane.
Sequence similarities	Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.

Ontologies

Keywords
Biological process	Ion transport Iron transport Transport
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	FAD Flavoprotein Iron NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	iron ion transport Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-lysine 6-monooxygenase (NADPH) activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 425	425	L-lysine 6-monooxygenase		PRO_0000204028
Regions
	Nucleotide binding	8 – 14	7	FAD Potential
Experimental info
	Mutagenesis	14	1	P → G: Low activity. Ref.3
	Sequence conflict	139	1	E → Q in AAA23196. Ref.1
	Sequence conflict	172	1	M → S in AAA23196. Ref.1
	Sequence conflict	231	1	E → D in AAA23196. Ref.1
	Sequence conflict	258 – 267	10	MTSDGITADS → TDIGWHHCPIL in AAA23196. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P11295-1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: 0F8B2A2F87E39751	FASTA	425	48,726
	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

References

[1]	"Nucleotide sequence of the iucD gene of the pColV-K30 aerobactin operon and topology of its product studied with phoA and lacZ gene fusions." Herrero M., de Lorenzo V., Neilands J.B. J. Bacteriol. 170:56-64(1988) [PubMed: 3275632] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15.
[2]	Marrone L., Viswanatha T. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Studies with lysine N6-hydroxylase. Effect of a mutation in the assumed FAD binding site on coenzyme affinities and on lysine hydroxylating activity." Stehr M., Smau L., Singh M., Seth O., Macheroux P., Ghisla S., Diekmann H. Biol. Chem. 380:47-54(1999) [PubMed: 10064136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF PRO-14. Strain: K-311.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M18968 Genomic DNA. Translation: AAA23196.1. U90207 Genomic DNA. Translation: AAC00523.1. AF016586 Genomic DNA. Translation: AAB71391.1. AF016587 Genomic DNA. Translation: AAB71392.1.
PIR	BVECID. A28665.
RefSeq	YP_002527487.1. YP_002539373.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7324509. 7379560.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-11590.
BRENDA	1.14.13.59. 246.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

IUCD_ECOLX

Accession

Primary (citable) accession number: P11295
Secondary accession number(s): O06897, O30770

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	December 15, 1998
Last modified:	June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)