FNO_ARCFU
ID FNO_ARCFU Reviewed; 212 AA.
AC O29370;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 {ECO:0000303|PubMed:11726492};
GN Name=fno; OrderedLocusNames=AF_0892;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX DOI=10.1007/BF00249125;
RA Kunow J., Schworer B., Stetter K.O., Thauer R.K.;
RT "A F420-dependent NADP reductase in the extremely thermophilic sulfate-
RT reducing Archaeoglobus fulgidus.";
RL Arch. Microbiol. 160:199-205(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP F420 AND NADP, FUNCTION, AND SUBUNIT.
RX PubMed=11726492; DOI=10.1093/emboj/20.23.6561;
RA Warkentin E., Mamat B., Sordel-Klippert M., Wicke M., Thauer R.K.,
RA Iwata M., Iwata S., Ermler U., Shima S.;
RT "Structures of F420H2:NADP+ oxidoreductase with and without its substrates
RT bound.";
RL EMBO J. 20:6561-6569(2001).
CC -!- FUNCTION: Catalyzes the reversible reduction of NADP(+) by F420H(2). In
CC this reaction the proS hydrogen at C5 of F420 is transferred into the
CC proS position at C4 of NADPH. {ECO:0000269|PubMed:11726492,
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=20 uM for reduced coenzyme F420 (at pH 8.0 and 65 degrees Celsius)
CC {ECO:0000269|Ref.2};
CC KM=40 uM for NADP(+) (at pH 8.0 and 65 degrees Celsius)
CC {ECO:0000269|Ref.2};
CC KM=10 uM for oxidized coenzyme F420 (at pH 5.5 and 65 degrees
CC Celsius) {ECO:0000269|Ref.2};
CC KM=40 uM for NADPH (at pH 5.5 and 65 degrees Celsius)
CC {ECO:0000269|Ref.2};
CC Vmax=660 umol/min/mg enzyme for NADP reduction with F420H(2) (at pH
CC 5.5 and 80 degrees Celsius) {ECO:0000269|Ref.2};
CC pH dependence:
CC Optimum pH is 8.0 for NADP reduction with F420H(2). Optimum pH is 5.5
CC for F420 reduction with NADPH. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius. Is highly thermostable.
CC {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11726492, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the F420-dependent NADP reductase family.
CC {ECO:0000305}.
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DR EMBL; AE000782; AAB90348.1; -; Genomic_DNA.
DR PIR; D69361; D69361.
DR RefSeq; WP_010878392.1; NC_000917.1.
DR PDB; 1JAX; X-ray; 1.80 A; A/B=1-212.
DR PDB; 1JAY; X-ray; 1.65 A; A/B=1-212.
DR PDBsum; 1JAX; -.
DR PDBsum; 1JAY; -.
DR AlphaFoldDB; O29370; -.
DR SMR; O29370; -.
DR STRING; 224325.AF_0892; -.
DR EnsemblBacteria; AAB90348; AAB90348; AF_0892.
DR GeneID; 1484115; -.
DR KEGG; afu:AF_0892; -.
DR eggNOG; arCOG00457; Archaea.
DR HOGENOM; CLU_076368_1_1_2; -.
DR OMA; IDTDVMV; -.
DR OrthoDB; 83005at2157; -.
DR PhylomeDB; O29370; -.
DR BRENDA; 1.5.1.40; 414.
DR EvolutionaryTrace; O29370; -.
DR Proteomes; UP000002199; 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 3D-structure; NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..212
FT /note="F420-dependent NADP reductase"
FT /id="PRO_0000419113"
FT BINDING 9..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11726492"
FT BINDING 31..32
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11726492"
FT BINDING 36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11726492"
FT BINDING 72
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11726492"
FT BINDING 76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11726492"
FT BINDING 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11726492"
FT BINDING 137
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11726492"
FT BINDING 207
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000269|PubMed:11726492"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1JAY"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1JAY"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:1JAY"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:1JAY"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:1JAY"
FT HELIX 34..48
FT /evidence="ECO:0007829|PDB:1JAY"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1JAY"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:1JAY"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1JAY"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1JAY"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:1JAY"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1JAY"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1JAX"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1JAX"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:1JAY"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1JAY"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:1JAY"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:1JAY"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:1JAY"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:1JAY"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1JAY"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:1JAY"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:1JAY"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1JAY"
SQ SEQUENCE 212 AA; 22865 MW; 16E2F079C9F471CE CRC64;
MRVALLGGTG NLGKGLALRL ATLGHEIVVG SRREEKAEAK AAEYRRIAGD ASITGMKNED
AAEACDIAVL TIPWEHAIDT ARDLKNILRE KIVVSPLVPV SRGAKGFTYS SERSAAEIVA
EVLESEKVVS ALHTIPAARF ANLDEKFDWD VPVCGDDDES KKVVMSLISE IDGLRPLDAG
PLSNSRLVES LTPLILNIMR FNGMGELGIK FL
