ID A6W2F9_MARMS Unreviewed; 242 AA.
AC A6W2F9;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Oxidoreductase FAD/NAD(P)-binding domain protein {ECO:0000313|EMBL:ABR72888.1};
GN OrderedLocusNames=Mmwyl1_3992 {ECO:0000313|EMBL:ABR72888.1};
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR72888.1};
RN [1] {ECO:0000313|EMBL:ABR72888.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR72888.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) 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 ---------------------------------------------------------------------------
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; CP000749; ABR72888.1; -; Genomic_DNA.
DR AlphaFoldDB; A6W2F9; -.
DR STRING; 400668.Mmwyl1_3992; -.
DR KEGG; mmw:Mmwyl1_3992; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_7_4_6; -.
DR OrthoDB; 9806195at2; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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}.
FT DOMAIN 1..98
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 242 AA; 26433 MW; BAA094F5F854D4DE CRC64;
MKEITATVNA VESINPNVYQ ITLKVDDLTF EAGQYLIVAL PTGEQVPYSI GSAPHELPYL
TLYVLVSDSA SLASKVVEHI KSNNSITIKA PGGDCHIANG ALDSTPENIL LIAGGTGFAQ
IKSLYSHLVE QNFTGNVSFY WGLRTPEDVF AQEWLEEAHK YTPFTLDVIV NEKGDKWHGR
SGWLYEAVLA DHPDLSKSVA FISGSVGMVY GTLDQLELKG LSKENCFSDV FAYAPHPDKP
VL
//