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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//