ID   A0A3N2E0B2_9GAMM        Unreviewed;       563 AA.
AC   A0A3N2E0B2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=NAD(P)H-flavin reductase {ECO:0000313|EMBL:ROS05457.1};
GN   ORFNames=EDC56_0987 {ECO:0000313|EMBL:ROS05457.1};
OS   Sinobacterium caligoides.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; Sinobacterium.
OX   NCBI_TaxID=933926 {ECO:0000313|EMBL:ROS05457.1, ECO:0000313|Proteomes:UP000275394};
RN   [1] {ECO:0000313|EMBL:ROS05457.1, ECO:0000313|Proteomes:UP000275394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100316 {ECO:0000313|EMBL:ROS05457.1,
RC   ECO:0000313|Proteomes:UP000275394};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:ROS05457.1}.
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DR   EMBL; RKHR01000003; ROS05457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2E0B2; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000275394; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd06186; NOX_Duox_like_FAD_NADP; 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; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972:SF69; METALLOREDUCTASE AIM14-RELATED; 1.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275394};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        241..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          314..417
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   563 AA;  65144 MW;  65440AE53FB1DEC8 CRC64;
     MKESLELQEK TPRGGLSSLG LQTRLTLFYL GQKYRPWLAF PWLLLLAVAL LSQFYLGYRY
     NSNDTTNIYL QLARGCSYTL LLVLCLLWLP VMRHGLAALW RSRWASWLPL EQAKNVHRWL
     GHLMMAGAMV HGACYLLYFN TLDAPFMDVL FGTESDVVRS MRTTMYEFVS EDESIDDVID
     WIDQGRPEQM FHDVIRPIMK EDCTKCHSAS STMTYAIPSL PLSYFDDVVA LSQRGIYSRQ
     FRINVCGLLM LLMLLPLWFT SLAVMRRRQH HVFQNIHRLG YLMVVLALLH IPRYNWLLVP
     AIILALEYFL SHYVRIYRGC HARMVRVSEG MLRLEMQRPD GFVIEPGHYL QLRVPKLGRY
     EWHDFSLTGG REGDDVIVLK IKAQGDWSDA LYDQLGNDGR AELDVDIRGP FASPAARPTR
     RREPILMVAG GIGITPFLGL LYTMLFDSVK RRPFHLVWVL RDGKLLEWLE PFLSSPLIAG
     GRIHLFLTQD EGADALPAWL QQQDVHGDRV VFYQHRPDLE RLFSDVSEEL ERPHCFVCGP
     EEMTRAVAAQ CRKRGWVMSI ERF
//