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Database: UniProt
Entry: R0FSG6_9BRAS
LinkDB: R0FSG6_9BRAS
Original site: R0FSG6_9BRAS 
ID   R0FSG6_9BRAS            Unreviewed;       200 AA.
AC   R0FSG6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=NAD(P)H dehydrogenase (quinone) {ECO:0000256|ARBA:ARBA00012648};
DE            EC=1.6.5.2 {ECO:0000256|ARBA:ARBA00012648};
GN   ORFNames=CARUB_v10019149mg {ECO:0000313|EMBL:EOA25782.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA25782.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC         Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000882};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC         Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000139};
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DR   EMBL; KB870809; EOA25782.1; -; Genomic_DNA.
DR   RefSeq; XP_006292884.1; XM_006292822.1.
DR   AlphaFoldDB; R0FSG6; -.
DR   STRING; 81985.R0FSG6; -.
DR   eggNOG; KOG4530; Eukaryota.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR005025; FMN_Rdtase-like.
DR   PANTHER; PTHR30543; CHROMATE REDUCTASE; 1.
DR   PANTHER; PTHR30543:SF21; NAD(P)H-DEPENDENT FMN REDUCTASE LOT6; 1.
DR   Pfam; PF03358; FMN_red; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121}.
FT   DOMAIN          11..157
FT                   /note="NADPH-dependent FMN reductase-like"
FT                   /evidence="ECO:0000259|Pfam:PF03358"
SQ   SEQUENCE   200 AA;  22016 MW;  92473DA1BF216767 CRC64;
     MEAVTAVKPL IRVAALSGSL RKTSCHTGLL RAAIDMTKES VPGMEIEYID ISLLPLINTD
     LEINGTYPPV VEAFRRKILE ADCVLFASPE YNFSVSAPLK NALDWASRAP NVWADKAAAI
     ISTGGSSGGG RAQYHLRQIG VFLDLHFINK PEFTLNAFQL PKKFDAEGNL IDEAAKEKLK
     QVLISLQAFT LRLQRLTIYI
//
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