FNO_METTH
ID FNO_METTH Reviewed; 232 AA.
AC O26350;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=F420-dependent NADP reductase {ECO:0000303|Ref.2};
DE EC=1.5.1.40 {ECO:0000269|Ref.2};
DE AltName: Full=F420H2:NADP oxidoreductase;
GN Name=fno; OrderedLocusNames=MTH_248;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX DOI=10.1016/0304-4165(84)90364-7;
RA Eirich L.D., Dugger R.S.;
RT "Purification and properties of an F420-dependent NADP reductase from
RT methanobacterium thermoautotrophicum.";
RL Biochim. Biophys. Acta 802:454-458(1984).
CC -!- FUNCTION: Catalyzes the reduction of NADP(+) with F420H(2) via hydride
CC transfer, and likely the reverse reaction, i.e. the reduction of F420
CC with NADPH. Probably functions in the regeneration of NADPH required in
CC biosynthetic reactions. Is specific for reduced F420 as electron donor
CC for the reduction of NADP; neither reduced FAD nor FMN can act as
CC electron donor. The enzyme is also specific for NADP; NAD is not
CC utilized as substrate. {ECO:0000250|UniProtKB:D9PVP5,
CC ECO:0000269|Ref.2}.
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:0000269|Ref.2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=128 uM for reduced coenzyme F420 {ECO:0000269|Ref.2};
CC KM=40 uM for NADP(+) {ECO:0000269|Ref.2};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Is extremely thermostable.
CC No detectable activity is lost when the enzyme is incubated at 65
CC degrees Celsius for 4 hours. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the F420-dependent NADP reductase family.
CC {ECO:0000305}.
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DR EMBL; AE000666; AAB84754.1; -; Genomic_DNA.
DR PIR; A69131; A69131.
DR AlphaFoldDB; O26350; -.
DR SMR; O26350; -.
DR STRING; 187420.MTH_248; -.
DR EnsemblBacteria; AAB84754; AAB84754; MTH_248.
DR KEGG; mth:MTH_248; -.
DR PATRIC; fig|187420.15.peg.217; -.
DR HOGENOM; CLU_076368_1_0_2; -.
DR OMA; ARYNEDM; -.
DR Proteomes; UP000005223; Chromosome.
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:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0052808; F:reduced coenzyme F420:NADP+ oxidoreductase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..232
FT /note="F420-dependent NADP reductase"
FT /id="PRO_0000087154"
FT BINDING 15..18
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O29370"
FT BINDING 37..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O29370"
FT BINDING 42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O29370"
FT BINDING 80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O29370"
FT BINDING 106
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O29370"
FT BINDING 151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O29370"
SQ SEQUENCE 232 AA; 24539 MW; A1CE60ABC8474296 CRC64;
MIKVMVMKIA VIGGTGDQGL GLALRFAVAG EEVIIGSRDA EKASKAASKV LEIAGRDDIS
VEGATNPDAA ASADVVVLTV PLQAQMVTLA SIRDQVRDKV LIDATVPIDS CIGGSAVRYI
DLWEGSAAER AARFLREQGT RVAAAFNNIS ASALLEVSEP VDCDCLVASD HRDALEVAAE
LAEKIDGVRA IECGGLENAR IIEKITPLLI NLNIRNRVRN AGIRITNLPE QE
