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Database: UniProt
Entry: A0A3N4NI69_9FLAO
LinkDB: A0A3N4NI69_9FLAO
Original site: A0A3N4NI69_9FLAO 
ID   A0A3N4NI69_9FLAO        Unreviewed;       734 AA.
AC   A0A3N4NI69;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:RPD91199.1};
GN   ORFNames=EGM88_14770 {ECO:0000313|EMBL:RPD91199.1};
OS   Aureibaculum marinum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aureibaculum.
OX   NCBI_TaxID=2487930 {ECO:0000313|EMBL:RPD91199.1, ECO:0000313|Proteomes:UP000270856};
RN   [1] {ECO:0000313|EMBL:RPD91199.1, ECO:0000313|Proteomes:UP000270856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH-SD17 {ECO:0000313|EMBL:RPD91199.1,
RC   ECO:0000313|Proteomes:UP000270856};
RA   Ji X.;
RT   "Aureibaculum marinum gen. nov., sp. nov., a member of the family
RT   Flavobacteriaceae isolated from the Bohai Sea.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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:RPD91199.1}.
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DR   EMBL; RPFJ01000074; RPD91199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4NI69; -.
DR   OrthoDB; 9789468at2; -.
DR   Proteomes; UP000270856; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR005625; PepSY-ass_TM.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF03929; PepSY_TM; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000270856};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        171..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          340..479
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          494..595
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   734 AA;  83890 MW;  173754BF4FAC4839 CRC64;
     MTISIWRYSH LALAISSSIF ILLASLTGII LAFEPISNRV QKQTISNLDE ISVAEITTTL
     RENYSEIISV EIDKNDWVTA SVIDDDGNNQ IFYIDPLTGK NIGTPTETHP IFQFATSLHR
     SLFLKSIGRF FVGLTSFLLF LISITGIFLI FKKQGGFRGF FKPIVKEKFN PYYHTLFGKW
     LLIPIVIITI SGVYLSLEQF SIISKTKIVH QEDTLFAEEP VLPLSEFDIF NNTKLSDVRK
     IEFPFAEFPD SYFLLQLKDK ELLINQFNGN IVSEVNYPFT AIISYYSLIF HTGQASIIWS
     IVLLFACIGI LFFMYSGFSI ALQRRKSRIK NRYKKDDCEY VILIGSENGN TFYFANALHS
     ELIRLGKKSY LAELNSYSSY KNMQHLVVMT ATYGAGEAPT NAKKFKALLQ THQQGKPFDY
     SVVGFGSLAY PDFCKYAYDV DELLEAHPNS NKIDDVFTIN NQSLESFNQW LLKWKEKENL
     EIRLPEAILS KKKRKTYTFE VIKNTKANKQ SDNTFLIQLK VTLGKVRFKS GDLLSITSDK
     DQRERLYSIG KWDRNTILIS VKLHDRGYVS NKLNDLTVGD KLTCGIVKNK DFRLPKKAKN
     AVFIATGTGI GPYLGMMHEN NKKAVLQLYW GGRTKASFEL YKKEVATYIN NGNLQSLHLA
     LSQEQEEKVY VQHLLERDSE HIAKILKNKG VIMICGSVVM QKDVTDTLNE ICKKHLNKPL
     SYYQNKGTVL MDCY
//
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