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Database: UniProt
Entry: A0A101M6I2_9GAMM
LinkDB: A0A101M6I2_9GAMM
Original site: A0A101M6I2_9GAMM 
ID   A0A101M6I2_9GAMM        Unreviewed;       235 AA.
AC   A0A101M6I2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=NAD(P)H-flavin reductase {ECO:0000313|EMBL:KUM51774.1};
DE            EC=1.16.1.3 {ECO:0000313|EMBL:KUM51774.1};
GN   Name=fre {ECO:0000313|EMBL:KUM51774.1};
GN   ORFNames=AR688_07620 {ECO:0000313|EMBL:KUM51774.1};
OS   Rheinheimera sp. EpRS3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=1712383 {ECO:0000313|EMBL:KUM51774.1, ECO:0000313|Proteomes:UP000054239};
RN   [1] {ECO:0000313|Proteomes:UP000054239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS3 {ECO:0000313|Proteomes:UP000054239};
RA   Presta L., Bosi E., Fondi M., Maida I., Maggini V., Bogani P.,
RA   Firenzuoli F., Chiellini C., De Pascale D., Palma F., Di Pilato V.,
RA   Rossolini G., Mengoni A., Fani R.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00038177}.
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:KUM51774.1}.
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DR   EMBL; LNQS01000011; KUM51774.1; -; Genomic_DNA.
DR   RefSeq; WP_068237687.1; NZ_LNQS01000011.1.
DR   AlphaFoldDB; A0A101M6I2; -.
DR   OrthoDB; 9806195at2; -.
DR   Proteomes; UP000054239; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR   CDD; cd06189; flavin_oxioreductase; 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; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354:SF7; NAD(P)H-FLAVIN REDUCTASE; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
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   3: Inferred from homology;
KW   Luminescence {ECO:0000256|ARBA:ARBA00023223};
KW   Oxidoreductase {ECO:0000313|EMBL:KUM51774.1}.
FT   DOMAIN          1..102
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   235 AA;  25824 MW;  9CCBCB7A47F33352 CRC64;
     MTTISCNVDL IEALTPTVNR VLLTPAQPVS FASGQYLQLC LSDSDKRPFS IASIPGQRQL
     ELHIGGAVAD PYASQALAHL MQQHQQQLPV LAEIGLGNAQ FRADSERPLI LLAGGTGFSY
     IYSIAQTIAA ANIDRPVFMY WGVREQSALY HADIMQAWAA QNSKYRFIPV VQNPDDSWQG
     RSGMVHEAVL NDFVSLEAYD IYVAGPFAMA GVVRNAFIEQ GAQREHMFAD AFAYI
//
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