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Database: UniProt
Entry: S3Z3D2_9MICO
LinkDB: S3Z3D2_9MICO
Original site: S3Z3D2_9MICO 
ID   S3Z3D2_9MICO            Unreviewed;       483 AA.
AC   S3Z3D2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE            EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN   ORFNames=HMPREF1484_00896 {ECO:0000313|EMBL:EPH15265.1};
OS   Dermabacter sp. HFH0086.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Dermabacter.
OX   NCBI_TaxID=1203568 {ECO:0000313|EMBL:EPH15265.1, ECO:0000313|Proteomes:UP000014577};
RN   [1] {ECO:0000313|EMBL:EPH15265.1, ECO:0000313|Proteomes:UP000014577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HFH0086 {ECO:0000313|EMBL:EPH15265.1,
RC   ECO:0000313|Proteomes:UP000014577};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Dermabacter sp. HFH0086.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2
CC         oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.18.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001005};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000362-1};
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008312}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPH15265.1}.
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DR   EMBL; ATFO01000007; EPH15265.1; -; Genomic_DNA.
DR   RefSeq; WP_016663812.1; NZ_KE340308.1.
DR   AlphaFoldDB; S3Z3D2; -.
DR   STRING; 1203568.HMPREF1484_00896; -.
DR   PATRIC; fig|1203568.3.peg.871; -.
DR   eggNOG; COG0493; Bacteria.
DR   HOGENOM; CLU_024722_4_0_11; -.
DR   Proteomes; UP000014577; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR   PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11938:SF91; NADPH:ADRENODOXIN OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF000362; FNR; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000362-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000362-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014577}.
FT   DOMAIN          10..192
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   BINDING         20
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         55
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         161..164
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         205..206
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         217
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         383
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         390..392
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         390
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ   SEQUENCE   483 AA;  53842 MW;  5219575815B973FE CRC64;
     MTSTFTDIPF RIAVIGSGPA GVYAAETFNK TPHVKKGRLA IEVDIFDALP TPFGLIRYGV
     APDHPRIKGI TTALHRILDR RDMRFFGNVA FGTDLTLEDL RERYDAIIFA TGALKDAQLD
     IPGIDLEGSF GAADFVAWYD SNPDYPREWR LDAESVAVIG NGNVALDVSR MLAKSADELL
     ATEIADNVYE GLKASQITDV HVFGRRGPAQ VKFSPLETRE LAHPKGVQVI LDERDFAQIS
     DEEWERIRAD KRIDQVVSTF EGWLEAQKEL EASGAEPTDR DGGEVKRRLH LHFWHRPVEV
     VGEDGRVTGM RFERTRIADD GMLEGTGEIV EYDVQQVYRA VGYFGSELPG VPYDPVRGVI
     HNDEGRVTTA EGAVVPACYA NGWIKRGPVG LIGATKSDAI ETVTHMIEDI EEGVLEPCPD
     RDPDSIVRLL DERGIRYVDW DGWLRLHDHE IQAGAKRKDS DGNARPSLKE IDREQMIRIA
     RGE
//
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