FNO_METTM
ID FNO_METTM Reviewed; 224 AA.
AC D9PVP5; O59661;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=F420-dependent NADP reductase {ECO:0000305|PubMed:9821972};
DE EC=1.5.1.40 {ECO:0000269|PubMed:9821972};
DE AltName: Full=F420H2:NADP oxidoreductase {ECO:0000303|PubMed:9821972};
GN Name=fno {ECO:0000303|PubMed:9821972}; OrderedLocusNames=MTBMA_c06980;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, GENE NAME,
RP SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=9821972; DOI=10.1016/s0014-5793(98)01288-5;
RA Berk H., Thauer R.K.;
RT "F420H2:NADP oxidoreductase from Methanobacterium thermoautotrophicum:
RT identification of the encoding gene via functional overexpression in
RT Escherichia coli.";
RL FEBS Lett. 438:124-126(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
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:0000269|PubMed:9821972}.
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|PubMed:9821972};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for F420 (at pH 6.0) {ECO:0000269|PubMed:9821972};
CC KM=50 uM for NADPH (at pH 6.0) {ECO:0000269|PubMed:9821972};
CC KM=0.15 mM for F420H(2) (at pH 8.0) {ECO:0000269|PubMed:9821972};
CC KM=70 uM for NADP(+) (at pH 8.0) {ECO:0000269|PubMed:9821972};
CC Vmax=1500 umol/min/mg enzyme for F420 reduction with NADPH (at pH
CC 6.0) {ECO:0000269|PubMed:9821972};
CC Vmax=1100 umol/min/mg enzyme for NADP(+) reduction with F420H(2) (at
CC pH 8.0) {ECO:0000269|PubMed:9821972};
CC pH dependence:
CC Optimum pH is 3.5 for F420 reduction with NADPH, and 8.0 for NADP(+)
CC reduction with F420H(2). {ECO:0000269|PubMed:9821972};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9821972}.
CC -!- SIMILARITY: Belongs to the F420-dependent NADP reductase family.
CC {ECO:0000305}.
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DR EMBL; Y17210; CAA76687.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL58293.1; -; Genomic_DNA.
DR PIR; T10120; T10120.
DR RefSeq; WP_013295517.1; NC_014408.1.
DR AlphaFoldDB; D9PVP5; -.
DR SMR; D9PVP5; -.
DR STRING; 79929.MTBMA_c06980; -.
DR EnsemblBacteria; ADL58293; ADL58293; MTBMA_c06980.
DR GeneID; 9704406; -.
DR KEGG; mmg:MTBMA_c06980; -.
DR PATRIC; fig|79929.8.peg.683; -.
DR HOGENOM; CLU_076368_1_0_2; -.
DR OMA; IDTDVMV; -.
DR OrthoDB; 83005at2157; -.
DR BRENDA; 1.5.1.40; 3256.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0102261; F:8-hydroxy-5-deazaflavin:NADPH oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0070967; F:coenzyme F420 binding; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IDA:UniProtKB.
DR GO; GO:0052808; F:reduced coenzyme F420:NADP+ oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006740; P:NADPH regeneration; IDA:UniProtKB.
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.
FT CHAIN 1..224
FT /note="F420-dependent NADP reductase"
FT /id="PRO_0000403984"
FT BINDING 9..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O29370"
FT BINDING 31..32
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O29370"
FT BINDING 36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O29370"
FT BINDING 74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O29370"
FT BINDING 100
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O29370"
FT BINDING 145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O29370"
SQ SEQUENCE 224 AA; 23448 MW; 8B3514EC14BCB0CF CRC64;
MKIAVLGGTG DQGLGLALRL ALAGEEVIIG SRDAEKAVSA AQKVLEIAER DDLKVKGATN
AEAAEEAEVA ILTVPLQAQM ATLGSVKEAI KGKVLIDATV PIDSCLGGSA VRYIDLWDGS
AAERAARFLE DQGTRVAAAF NNISASALLD ITGPVDCDCL IASDHRDALD LASELAEKID
GVRAIDCGGL ENARVIEKIT PLLINLNIKN RIRNAGIRIT NLPE
