ID A0A143QDA2_9NOCA Unreviewed; 454 AA.
AC A0A143QDA2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 Name=pvdA {ECO:0000313|EMBL:AMY20387.1};
GN ORFNames=A3Q40_03025 {ECO:0000313|EMBL:AMY20387.1};
OS Rhodococcus sp. PBTS 1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY20387.1, ECO:0000313|Proteomes:UP000076180};
RN [1] {ECO:0000313|EMBL:AMY20387.1, ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY20387.1,
RC ECO:0000313|Proteomes:UP000076180};
RX PubMed=27284129;
RA Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL Submitted (APR-2016) 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; CP015219; AMY20387.1; -; Genomic_DNA.
DR RefSeq; WP_068103291.1; NZ_CP015219.1.
DR AlphaFoldDB; A0A143QDA2; -.
DR STRING; 1653478.A3Q40_03025; -.
DR KEGG; rhu:A3Q40_03025; -.
DR PATRIC; fig|1653478.3.peg.3065; -.
DR Proteomes; UP000076180; 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 PANTHER; PTHR42802:SF1; L-ORNITHINE N(5)-MONOOXYGENASE; 1.
DR PANTHER; PTHR42802; MONOOXYGENASE; 1.
DR Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:AMY20387.1};
KW Oxidoreductase {ECO:0000313|EMBL:AMY20387.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076180}.
FT REGION 435..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 49801 MW; 15CB9F2BCF5AF91A CRC64;
MTGDDTLDVV GIGFGPANLA LAIAIEEHNR SCAPGEQVRA IFVERQDAFG WHPGMLLEGA
TMQIAFPKDL ATFRNPSSEY TFFQYLFARG RLVDFVNHQT FFPTRLEFHD YLSWAADRVD
ADVCYGTSVT AVRRVGDELV VQCDDGRVLH TRNVAVGAGL QQRVPEWATL SARCFHNHDF
LGRMAELPRP THGRFAVLGA GQSAAEVVQY LHAHHPHAEV HSIFARYGYS PADDSPYANR
IFDPEAVDEL HRAPADERAR LLALHRSTNY SVVDLELIEE LYRTEYAERV SGHRRLFMRR
ASTIDAAVET ADGIEVTVRD GIDGIADTLV CDALVLATGF RPSPLRPLLG DLAPDDDAPR
VVTRDYRLVA GEDGDGVDGV GAADDGRTAV YLQGGTESTH GITSSLLSNV AVRSGEILHS
VLVRRAGSAT LARVDRTADR RDRPAPTFAV SEAR
//
