ID A0R0U3_MYCS2 Unreviewed; 435 AA.
AC A0R0U3;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=L-lysine N6-monooxygenase MbtG {ECO:0000256|ARBA:ARBA00016406};
DE EC=1.14.13.59 {ECO:0000256|ARBA:ARBA00013076};
DE AltName: Full=Lysine 6-N-hydroxylase {ECO:0000256|ARBA:ARBA00032738};
DE AltName: Full=Lysine N6-hydroxylase {ECO:0000256|ARBA:ARBA00032493};
DE AltName: Full=Lysine-N-oxygenase {ECO:0000256|ARBA:ARBA00029939};
DE AltName: Full=Mycobactin synthase protein G {ECO:0000256|ARBA:ARBA00031158};
GN OrderedLocusNames=MSMEG_4509 {ECO:0000313|EMBL:ABK70003.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK70003.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK70003.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000168};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005102}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000256|ARBA:ARBA00007588}.
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DR EMBL; CP000480; ABK70003.1; -; Genomic_DNA.
DR RefSeq; WP_011729884.1; NZ_SIJM01000026.1.
DR RefSeq; YP_888781.1; NC_008596.1.
DR AlphaFoldDB; A0R0U3; -.
DR STRING; 246196.MSMEG_4509; -.
DR PaxDb; 246196-MSMEI_4397; -.
DR GeneID; 66735837; -.
DR KEGG; msm:MSMEG_4509; -.
DR PATRIC; fig|246196.19.peg.4412; -.
DR eggNOG; COG3486; Bacteria.
DR OrthoDB; 9149460at2; -.
DR Proteomes; UP000000757; Chromosome.
DR GO; GO:0047091; F:L-lysine 6-monooxygenase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR025700; Lys/Orn_oxygenase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43539:SF78; FAD-DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757}.
SQ SEQUENCE 435 AA; 47488 MW; FF00DC1917F38FEB CRC64;
MSETTPRLAV IGAGPKGIAV AAKAAELRAM GAAAPEVVVI DRAGVAANWQ AVGGWTDGQH
RLGTSPEKDV GFPYRSSLVP RRNAELDERM MRHSWQSYLV DIGQFAEWID RGRPAPTHRR
WSQYLNWVAD NIGMSLITGE VTRIGLGDDQ NSWTLHTHED TVAADAVMIT GPGQAERSIL
PGNPRVLSIA QFWHRAAANE LISAERVAVI GGGETAATML NELFRHRVSA ITVISPQVTL
FTRGESFFEN TLYSDPTHWA GLTLDERRDA MNRTDRGVFS ARVQESLLAD DRIRHLRGRV
AHAVARDEKI RLTLQTNSGS ERLETVHGFD LVIDGSGADA LWFVPLLAQD ALDKLELGLG
RPLTGDTLQE SIGYDLAVTG VTPKLFLPGL AGLNQGPGFP NLSCLGLLSD RVLGAEMSVT
TDRTIRRTDE HQSVR
//
