ID E4PGR7_MARAH Unreviewed; 508 AA.
AC E4PGR7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Monooxygenase, flavin-binding family protein {ECO:0000313|EMBL:ADP99376.1};
GN OrderedLocusNames=HP15_3612 {ECO:0000313|EMBL:ADP99376.1};
OS Marinobacter adhaerens (strain DSM 23420 / HP15).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP99376.1, ECO:0000313|Proteomes:UP000007077};
RN [1] {ECO:0000313|EMBL:ADP99376.1, ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX PubMed=21304739;
RA Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA Glockner F.O., Grossart H.P., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT diatom-interacting marine microorganism.";
RL Stand. Genomic Sci. 3:97-107(2010).
RN [2] {ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA Gloeckner F.O., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
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DR EMBL; CP001978; ADP99376.1; -; Genomic_DNA.
DR RefSeq; WP_014578764.1; NC_017506.1.
DR AlphaFoldDB; E4PGR7; -.
DR STRING; 225937.HP15_3612; -.
DR GeneID; 78558054; -.
DR KEGG; mad:HP15_3612; -.
DR PATRIC; fig|225937.3.peg.3641; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_032067_2_0_6; -.
DR OMA; LWNGVML; -.
DR Proteomes; UP000007077; Chromosome.
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; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR43872; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02570)-RELATED; 1.
DR PANTHER; PTHR43872:SF1; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02570)-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
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:0000313|EMBL:ADP99376.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 508 AA; 57176 MW; CEB081ED26F7371D CRC64;
MSNQHFDVLI IGAGVSGIGM ACHLKRECPG KSFAILERRQ SLGGTWDLFR YPGIRSDSDM
FTFGYNFRPW TGGKVLADGA SIKNYVAETA REHDVERHIR FGLAVKTADW SGVDKCWKLS
ALNEATGETE HYTANFMVGC TGYYNYDQGY KPDFPGENDF RGQVIHPQHW PEDLDYAGKK
VVVIGSGATA ITLVPTMAEK ASHVTMLQRS PTYLMPLPST DKVSLALQKI LPERTAYRLT
RARNISISRF LYLRSRRSPK FMRRLFLGII KRKVGDTADM RHFTPDYNPW DQRLCVVKDG
DLFQAMKAGK ASIATDHIDR FTETGIRLKS GEELEADIII PATGLDIQML GGIRPTVDGQ
EVVMKDKIIY KNVMVEGVPN AGMIFGYTNI SWTLKVDIAA EYLCRLMNLM DKRGYRTVVA
RDTENSRGDD TVLGSLDAGY IRRAADRLPR QGTHGPWKSS QNYLEDVRIL RFEPIEDGYL
EFDGKRTHAS HKESGGFLRP LRSALFGT
//