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Database: UniProt
Entry: A0A0W1KJ99_9ACTO
LinkDB: A0A0W1KJ99_9ACTO
Original site: A0A0W1KJ99_9ACTO 
ID   A0A0W1KJ99_9ACTO        Unreviewed;       472 AA.
AC   A0A0W1KJ99;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE            EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN   Name=fprA {ECO:0000313|EMBL:KTF04068.1};
GN   ORFNames=AQZ59_01044 {ECO:0000313|EMBL:KTF04068.1};
OS   Trueperella bernardiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Trueperella.
OX   NCBI_TaxID=59561 {ECO:0000313|EMBL:KTF04068.1, ECO:0000313|Proteomes:UP000054404};
RN   [1] {ECO:0000313|EMBL:KTF04068.1, ECO:0000313|Proteomes:UP000054404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCDC 89-0504 {ECO:0000313|EMBL:KTF04068.1,
RC   ECO:0000313|Proteomes:UP000054404};
RA   Bernier A.-M., Bernard K.;
RT   "Draft Genome Sequence of the Type Strain Trueperella bernardiae LCDC 89-
RT   0504T, Isolated from Blood Culture.";
RL   Submitted (NOV-2015) 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:KTF04068.1}.
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DR   EMBL; LNIZ01000004; KTF04068.1; -; Genomic_DNA.
DR   RefSeq; WP_062613605.1; NZ_JASPDQ010000005.1.
DR   AlphaFoldDB; A0A0W1KJ99; -.
DR   STRING; 59561.AQZ59_01044; -.
DR   PATRIC; fig|59561.3.peg.1034; -.
DR   OrthoDB; 289202at2; -.
DR   Proteomes; UP000054404; Unassembled WGS sequence.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:KTF04068.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054404}.
FT   DOMAIN          18..180
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   BINDING         27
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         56
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         92
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         206..207
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         218
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         370
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         377..379
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         377
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ   SEQUENCE   472 AA;  52246 MW;  41D95E2AC4C31313 CRC64;
     MPGARVDKGE SVADRPLHVA VIGAGPAGIY ASDILSKSGV EVKIDLYEKL PAPYGLVRYG
     VAPDHPRIKA IINALYNVLQ RGDIRLVGNV EIGRDITFHE LHEHYDAVII ATGADQDRPF
     NIPGSNLPEV YGAANFVYWY DGHPDYPRTW PLEAKEIAVL GVGNVALDVA RILAKHPDDL
     MVTEIPGNVE EGLRRSPVTD IHIFGRRGPA QVKFTPMELR ELGQVPDVDI IVYPEDFDYD
     AGSEKAMEES KMTRQVVEQL TEWVFQEPED LTASRRIHIH MLQQPAEILG DEHVEGIRME
     RTALQGDASV KGTGEFIDYP VQAVYRAVGY FSSEIPGAPY DAGRGIVPNV QGRVITTDGE
     VVPGMYATGW IKRGPVGLIG STKSDAQETI GHLVEDYEAG KLHATTDALG WEETSKVLDE
     RGVRYTTWRG WELLNEYEMA LGAERGRARL KVVERETMTA VSRGEEHDGK LY
//
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