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Database: UniProt
Entry: W7QJW4_9ALTE
LinkDB: W7QJW4_9ALTE
Original site: W7QJW4_9ALTE 
ID   W7QJW4_9ALTE            Unreviewed;       232 AA.
AC   W7QJW4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=FMN reductase {ECO:0000313|EMBL:EWH09257.1};
DE            EC=1.16.1.3 {ECO:0000313|EMBL:EWH09257.1};
GN   Name=fre {ECO:0000313|EMBL:EWH09257.1};
GN   ORFNames=DS2_13354 {ECO:0000313|EMBL:EWH09257.1};
OS   Catenovulum agarivorans DS-2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Catenovulum.
OX   NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH09257.1, ECO:0000313|Proteomes:UP000019276};
RN   [1] {ECO:0000313|EMBL:EWH09257.1, ECO:0000313|Proteomes:UP000019276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-2 {ECO:0000313|EMBL:EWH09257.1,
RC   ECO:0000313|Proteomes:UP000019276};
RX   PubMed=24604650;
RA   Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT   "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT   Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL   Genome Announc. 2:e00144-14(2014).
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
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:EWH09257.1}.
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DR   EMBL; ARZY01000026; EWH09257.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7QJW4; -.
DR   STRING; 1328313.DS2_13354; -.
DR   PATRIC; fig|1328313.3.peg.2728; -.
DR   eggNOG; COG0543; Bacteria.
DR   OrthoDB; 9806195at2; -.
DR   Proteomes; UP000019276; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; 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; IPR008333; Cbr1-like_FAD-bd_dom.
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; PF00970; FAD_binding_6; 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:EWH09257.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019276}.
FT   DOMAIN          1..98
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   232 AA;  25715 MW;  5728445C1B1C54AF CRC64;
     MLHQCEVIEI SPLTEFVYQV KLKPKQPFEF IAGQYIELLL SESDKRPFSI ANAPSKDGFI
     ELQIGAAVQD DYTSAAMAHL QNNSTVTIAG PSGNAGLRPY SQQPVILMAG GTGFSYTRSI
     ALALLQQKPT APVYLYWGLR NQAAAYELDF WYAQESANFK FIPVIENPDE NWSGRSGNVI
     DAVLADFPSL QDYQVYSAGR FEMVGKARKA FIEKGLSKDN VFADAFAFMD LD
//
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