IUCD_ECOLX
ID IUCD_ECOLX Reviewed; 425 AA.
AC P11295; O06897; O30770;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=L-lysine N6-monooxygenase;
DE EC=1.14.13.59 {ECO:0000269|PubMed:2935523};
DE AltName: Full=Lysine 6-N-hydroxylase;
DE AltName: Full=Lysine N6-hydroxylase;
DE AltName: Full=Lysine-N-oxygenase;
GN Name=iucD {ECO:0000303|PubMed:2935523}; Synonyms=aerA;
OS Escherichia coli.
OG Plasmid IncFI ColV3-K30, and Plasmid ColV-K311.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
RC PLASMID=IncFI ColV3-K30;
RX PubMed=3275632; DOI=10.1128/jb.170.1.56-64.1988;
RA Herrero M., de Lorenzo V., Neilands J.B.;
RT "Nucleotide sequence of the iucD gene of the pColV-K30 aerobactin operon
RT and topology of its product studied with phoA and lacZ gene fusions.";
RL J. Bacteriol. 170:56-64(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=IncFI ColV3-K30;
RA Marrone L., Viswanatha T.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF PRO-14.
RC STRAIN=K-311; PLASMID=ColV-K311;
RX PubMed=10064136; DOI=10.1515/bc.1999.006;
RA Stehr M., Smau L., Singh M., Seth O., Macheroux P., Ghisla S., Diekmann H.;
RT "Studies with lysine N6-hydroxylase. Effect of a mutation in the assumed
RT FAD binding site on coenzyme affinities and on lysine hydroxylating
RT activity.";
RL Biol. Chem. 380:47-54(1999).
RN [4]
RP FUNCTION AS A MONOOXYGENASE AND IN AEROBACTIN BIOSYNTHESIS, NOMENCLATURE,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=2935523; DOI=10.1128/jb.165.2.570-578.1986;
RA de Lorenzo V., Bindereif A., Paw B.H., Neilands J.B.;
RT "Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in
RT Escherichia coli K-12.";
RL J. Bacteriol. 165:570-578(1986).
CC -!- FUNCTION: Flavoprotein monooxygenase required for N-hydroxylation of
CC lysine. Involved in the biosynthesis of the siderophore aerobactin
CC which is a chelator that mediates the high-affinity iron transport
CC systems induced by the organism under iron-stressed conditions.
CC {ECO:0000269|PubMed:2935523}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysine + NADPH + O2 = H2O + N(6)-hydroxy-L-lysine + NADP(+);
CC Xref=Rhea:RHEA:23228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32551, ChEBI:CHEBI:57783, ChEBI:CHEBI:57820,
CC ChEBI:CHEBI:58349; EC=1.14.13.59;
CC Evidence={ECO:0000269|PubMed:2935523};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23229;
CC Evidence={ECO:0000269|PubMed:2935523};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:E9QYP0};
CC -!- PATHWAY: Siderophore biosynthesis; aerobactin biosynthesis.
CC {ECO:0000305|PubMed:2935523}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M18968; AAA23196.1; -; Genomic_DNA.
DR EMBL; U90207; AAC00523.1; -; Genomic_DNA.
DR EMBL; AF016586; AAB71391.1; -; Genomic_DNA.
DR EMBL; AF016587; AAB71392.1; -; Genomic_DNA.
DR PIR; A28665; BVECID.
DR RefSeq; WP_000750130.1; NZ_WWEV01000005.1.
DR RefSeq; YP_002527487.1; NC_011964.1.
DR RefSeq; YP_009071166.1; NC_025179.1.
DR AlphaFoldDB; P11295; -.
DR SMR; P11295; -.
DR PRIDE; P11295; -.
DR KEGG; ag:AAA23196; -.
DR OMA; YHGNTNY; -.
DR OrthoDB; 324612at2; -.
DR BioCyc; MetaCyc:MON-11590; -.
DR UniPathway; UPA00014; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047091; F:L-lysine 6-monooxygenase (NADPH) activity; IMP:UniProtKB.
DR GO; GO:0019270; P:aerobactin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR025700; Lys/Orn_oxygenase.
DR PANTHER; PTHR42802; PTHR42802; 1.
DR Pfam; PF13434; K_oxygenase; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein;
KW Membrane; NADP; Oxidoreductase; Plasmid.
FT CHAIN 1..425
FT /note="L-lysine N6-monooxygenase"
FT /id="PRO_0000204028"
FT BINDING 8..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT MUTAGEN 14
FT /note="P->G: Low activity."
FT /evidence="ECO:0000269|PubMed:10064136"
FT CONFLICT 139
FT /note="E -> Q (in Ref. 1; AAA23196)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="M -> S (in Ref. 1; AAA23196)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="E -> D (in Ref. 1; AAA23196)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..267
FT /note="MTSDGITADS -> TDIGWHHCPIL (in Ref. 1; AAA23196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 48726 MW; 0F8B2A2F87E39751 CRC64;
MKKSVDFIGV GTGPFNLSIA ALSHQIEELD CLFFDEHPHF SWHPGMLVPD CHMQTVFLKD
LVSAVAPTNP YSFVNYLVKH KKFYRFLTSR LRTVSREEFS DYLRWAAEDM NNLYFSHTVE
NIDFDKKRRL FLVQTSQGEY FARNICLGTG KQPYLPPCVK HMTQSCFHAS EMNLRRPDLS
GKRITVVGGG QSGADLFLNA LRGEWGEAAE INWVSRRNNF NALDEAAFAD EYFTPEYISG
FSGLEEDIRH QLLDEQKMTS DGITADSLLT IYRELYHRFE VLRKPRNIRL LPSRSVTTLE
SSGPGWKLLM EHHLDQGRES LESDVVIFAT GYRSALPQIL PSLMPLITMH DKNTFKVRDD
FTLEWSGPKE NNIFVVNASM QTHGIAEPQL SLMAWRSARI LNRVMGRDLF DLSMPPALIQ
WRSGT
