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FNO_METJA
ID   FNO_METJA               Reviewed;         223 AA.
AC   Q58896;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=F420-dependent NADP reductase;
DE            EC=1.5.1.40;
DE   AltName: Full=F420H2:NADP oxidoreductase;
GN   Name=fno; OrderedLocusNames=MJ1501;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Catalyzes the reduction of NADP(+) with F420H(2) via hydride
CC       transfer, and the reverse reaction, i.e. the reduction of F420 with
CC       NADPH. Probably functions in the regeneration of NADPH required in
CC       biosynthetic reactions. {ECO:0000250|UniProtKB:D9PVP5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) +
CC         NADPH + oxidized coenzyme F420-(gamma-L-Glu)(n);
CC         Xref=Rhea:RHEA:31363, Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:14378,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.5.1.40;
CC         Evidence={ECO:0000250|UniProtKB:D9PVP5};
CC   -!- SIMILARITY: Belongs to the F420-dependent NADP reductase family.
CC       {ECO:0000305}.
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DR   EMBL; L77117; AAB99514.1; -; Genomic_DNA.
DR   PIR; D64487; D64487.
DR   RefSeq; WP_010871024.1; NC_000909.1.
DR   AlphaFoldDB; Q58896; -.
DR   SMR; Q58896; -.
DR   STRING; 243232.MJ_1501; -.
DR   EnsemblBacteria; AAB99514; AAB99514; MJ_1501.
DR   GeneID; 1452408; -.
DR   KEGG; mja:MJ_1501; -.
DR   eggNOG; arCOG00457; Archaea.
DR   HOGENOM; CLU_076368_1_0_2; -.
DR   InParanoid; Q58896; -.
DR   OMA; IDTDVMV; -.
DR   OrthoDB; 83005at2157; -.
DR   PhylomeDB; Q58896; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0102261; F:8-hydroxy-5-deazaflavin:NADPH oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070967; F:coenzyme F420 binding; IEA:InterPro.
DR   GO; GO:0008823; F:cupric reductase activity; IBA:GO_Central.
DR   GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0052808; F:reduced coenzyme F420:NADP+ oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015677; P:copper ion import; IBA:GO_Central.
DR   GO; GO:0006740; P:NADPH regeneration; IEA:InterPro.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR010185; NpdG.
DR   InterPro; IPR028939; P5C_Rdtase_cat_N.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01915; npdG; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..223
FT                   /note="F420-dependent NADP reductase"
FT                   /id="PRO_0000087152"
FT   BINDING         9..12
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O29370"
FT   BINDING         30..31
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O29370"
FT   BINDING         35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O29370"
FT   BINDING         75
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O29370"
FT   BINDING         101
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O29370"
SQ   SEQUENCE   223 AA;  24068 MW;  2370BBD6F5BBD3D9 CRC64;
     MKIAILGGTG DQGFGLALRL AKNNKIIIGS RKKEKAEEAA KKAKEILKQR GIEADIIGLE
     NKDAAKEGDV VILSLPYEYT LSTIKQLKEE LKGKIVVSIG VPLATAIGDK PTRLLFPPDG
     SVAEMVQNVL KESKVVSAFQ NVCHAVLEDL DNPVDCDILV CGNDEEAKKV VIDLANQIDG
     VRAIDCGNLE KSRIIEAITP LLIGLNIKYK SKGTGIRITN LEI
 
 
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