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Database: UniProt
Entry: A0A1Z1WER4_9ACTN
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ID   A0A1Z1WER4_9ACTN        Unreviewed;       437 AA.
AC   A0A1Z1WER4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
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   ORFNames=SMD44_04356 {ECO:0000313|EMBL:ARX84899.1};
OS   Streptomyces alboflavus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX84899.1, ECO:0000313|Proteomes:UP000195880};
RN   [1] {ECO:0000313|EMBL:ARX84899.1, ECO:0000313|Proteomes:UP000195880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MDJK44 {ECO:0000313|EMBL:ARX84899.1,
RC   ECO:0000313|Proteomes:UP000195880};
RA   Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT   "Streptomyces alboflavus Genome sequencing and assembly.";
RL   Submitted (MAY-2017) 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC         H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00000849};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
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; CP021748; ARX84899.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z1WER4; -.
DR   STRING; 67267.GCA_000716675_07992; -.
DR   KEGG; salf:SMD44_04356; -.
DR   eggNOG; COG2072; Bacteria.
DR   OrthoDB; 9778740at2; -.
DR   Proteomes; UP000195880; 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; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000313|EMBL:ARX84899.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195880}.
SQ   SEQUENCE   437 AA;  46289 MW;  EFBD70FDE022BC57 CRC64;
     MHDLLIVGAG PYGLSIAAHA AASGLDVRVF GRPMASWRDH MPRGMFLKSE PWASDLSDPG
     ARYGLAAYCA REGLRAEHGV PLPVEHFAAY GLWFAEQAAP PVDERLIRSV RPLTDGFAVT
     TADGETCHGR TVALAVGVMP FVEIPSLVRD LGPDHVSHSS HHADLGPLRD KDVTVLGAGQ
     AALETAALLA EQGTRVRVLA RAPQVRWNTL PPALRRPWWQ SASAPHSGLG CGWRNWFYAE
     RPGLFRLLPE PTRARVCATA LGPAGAWWVR DRVEAGPCGA PTAGGAARSA AAIEIVTGHR
     LTGARRHDGQ VLLSTHGPDG AAVFETDHVL AATGFRALTH RIDVLDLDVR DTLRQLADGA
     PYVDTAFETS LPGLFVAGLP TASSFGPAMR FVQGAGFTAA RLVAGVRRRV RRPGAVPVAR
     GTGAAAPVPY ESGAPGR
//
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