ID A0A1J6WF85_9BACI Unreviewed; 432 AA.
AC A0A1J6WF85;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Ornithine monooxygenase {ECO:0000313|EMBL:OIU70536.1};
GN ORFNames=BHE18_11940 {ECO:0000313|EMBL:OIU70536.1};
OS Rossellomorea aquimaris.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=189382 {ECO:0000313|EMBL:OIU70536.1, ECO:0000313|Proteomes:UP000182062};
RN [1] {ECO:0000313|EMBL:OIU70536.1, ECO:0000313|Proteomes:UP000182062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAMM {ECO:0000313|EMBL:OIU70536.1,
RC ECO:0000313|Proteomes:UP000182062};
RA Waghmode S.R., Suryavanshi M.V.;
RT "Bacillus aquimaris SAMM genome sequence reveals colonization and
RT biosurfactant production capacities.";
RL Submitted (SEP-2016) 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:OIU70536.1}.
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DR EMBL; MINN01000106; OIU70536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J6WF85; -.
DR OrthoDB; 7527071at2; -.
DR Proteomes; UP000182062; 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; 1.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:OIU70536.1};
KW Oxidoreductase {ECO:0000313|EMBL:OIU70536.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000182062}.
SQ SEQUENCE 432 AA; 49947 MW; D84209F918C7DE27 CRC64;
MLDCIGIGIG PYNLSLAALM DEKTDLKVKF FDKTPEFQWY PGMLIDLTDL QVPFIADLVT
FANPQSRYSY LNYLHTHNRL YKFFFFHKFE MPRQEYNDYA RWVVKQLPHC QFHSEVIGVK
DTGDYFEVEV RNGLTDECEV YKAKHVVMGT GSKPLILDGM EGLPPEDVHH TSSYLFHKES
TLESSSITII GSGQSAAEVF HDLLKEQRDH PYKLTWMTRS EGILQLESSK LGQEFFAPDY
VDYFHGLSFE KRLEALKTLD QLRNGIDMDT LNNIYNILYH HSVSEDAPDI VIQPLTEVNK
VRQEEEGYVL DCRQWQEERE FSYVSGKVIL ATGYVPNIPS WFDDAFGDEI VWEDDKRFKV
SRDYKLVFKN GAERSHHFYT LTNLEHSHGA GATNLGLSVD RNIAIINDIT GKEVYKVQRN
TIFSQFSMGD SE
//
