ID A0A3A9ZK95_9ACTN Unreviewed; 506 AA.
AC A0A3A9ZK95;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=NAD(P)/FAD-dependent oxidoreductase {ECO:0000313|EMBL:RKN47746.1};
GN ORFNames=D7223_13435 {ECO:0000313|EMBL:RKN47746.1};
OS Micromonospora endolithica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=230091 {ECO:0000313|EMBL:RKN47746.1, ECO:0000313|Proteomes:UP000281726};
RN [1] {ECO:0000313|EMBL:RKN47746.1, ECO:0000313|Proteomes:UP000281726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12677 {ECO:0000313|EMBL:RKN47746.1,
RC ECO:0000313|Proteomes:UP000281726};
RX PubMed=15046305; DOI=10.1078/072320204322881781;
RA Hirsch P., Mevs U., Kroppenstedt R.M., Schumann P., Stackebrandt E.;
RT "Cryptoendolithic actinomycetes from antarctic sandstone rock samples:
RT Micromonospora endolithica sp. nov. and two isolates related to
RT Micromonospora coerulea Jensen 1932.";
RL Syst. Appl. Microbiol. 27:166-174(2004).
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:RKN47746.1}.
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DR EMBL; RBAK01000004; RKN47746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9ZK95; -.
DR OrthoDB; 5168853at2; -.
DR Proteomes; UP000281726; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 2.
DR PIRSF; PIRSF000332; FMO; 2.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000281726}.
SQ SEQUENCE 506 AA; 55605 MW; 3A137EF9B33F5B87 CRC64;
MRIAIVGAGF AGLGAAKVLR QSGFDVTVFE KAPDVGGVWS RTRRYPGLST QNNRDTYHFS
DLPMPSHWPE WPTGEQVQQY LESYADTFGL RDVVRLSTEV VAAELVADET EWSIGSRPAG
GGEPATWERY DHLVVANGIF SEPFIPAFPG RQEFTAAGGR VLAAGEFHDV EAARGRNVLV
VGYGKSSCDV AVPVSDVAAH TDVVARGLLW KMPKKLAGRL NYKYLTLTRL GEGLFRYLDP
KGVERFLHGP GNGLRRGMLD SIGAVATRQL KLRELGLVPD GSFEDIARST VSLATEGFFE
RVADGRITVH RDQVIGELLV DAGRPAARLT DGTVLAADLV ICGTGFRQRV PFFDETLHAR
LEDGAGNFAL YRHILPIDVP RLTFAGYNSS FFSPLSAEMA AVWTAAHLRG GVTLPSRERM
REDVRRRLAW MVERTDGRHA RGTNIIPFSM HNIDELLDEL GLNVGRLTRA RQWLLPVDPR
SYRGVTARML ARTGGSVRRS AVGDPV
//
