ID A6CYH1_9VIBR Unreviewed; 445 AA.
AC A6CYH1;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=L-lysine 6-monooxygenase {ECO:0000313|EMBL:EDL54669.1};
GN ORFNames=VSAK1_20969 {ECO:0000313|EMBL:EDL54669.1};
OS Vibrio mediterranei AK1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=391591 {ECO:0000313|EMBL:EDL54669.1, ECO:0000313|Proteomes:UP000003769};
RN [1] {ECO:0000313|EMBL:EDL54669.1, ECO:0000313|Proteomes:UP000003769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EDL54669.1,
RC ECO:0000313|Proteomes:UP000003769};
RA Rosenberg E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDL54669.1}.
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DR EMBL; ABCH01000006; EDL54669.1; -; Genomic_DNA.
DR RefSeq; WP_006070380.1; NZ_ABCH01000006.1.
DR AlphaFoldDB; A6CYH1; -.
DR Proteomes; UP000003769; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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:EDL54669.1};
KW Oxidoreductase {ECO:0000313|EMBL:EDL54669.1}.
SQ SEQUENCE 445 AA; 50231 MW; B586688B46D75B13 CRC64;
MANSKQHEIY DLVGIGAGPF NLSIAALSNE VNTLKTVFLE ARSEFSWHPG LLLDGANMQT
HFLKDLVSAV CPTSEYSFLN YLVSNKKYYR FLSTEQSCIS RQEFSDYLSW ASKNMPNVVF
DSAVQNIEKH DGLYHIHTKD LVYRARHICL GTGKTPYFPE CTKPSLGANV FHAAEIGLRE
RNLTGRRVTI IGGGQSGADI FLNVLREKWG KPSHLNWVTR RANYQPLDEA AFTNEYFTPE
YVDTFIGLND KVKQREIAHQ KLTSDGVTQK CLLEIYQELY QRFDVMKEKR WIELLPHRTL
TALEETSQGL KLKYANAITE TDEEDNADIV ILATGYQGQL PSCAKALESS FKRDQNRQIR
LNGAFSIEMS DSDEIGNVFV VNAGLHSHGI AEPQLSLAAW RAAKIINQVA DQAAFDIEAV
NGLMNWGNIN MERYEDRALK ELATS
//
