ID S0DPI7_GIBF5 Unreviewed; 603 AA.
AC S0DPI7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 08-NOV-2023, entry version 42.
DE RecName: Full=NADPH-dependent diflavin oxidoreductase 1 {ECO:0000256|HAMAP-Rule:MF_03178};
DE EC=1.18.1.- {ECO:0000256|HAMAP-Rule:MF_03178};
DE AltName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03178};
GN Name=TAH18 {ECO:0000256|HAMAP-Rule:MF_03178};
GN ORFNames=FFUJ_04425 {ECO:0000313|EMBL:CCT64360.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT64360.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|EMBL:CCT64360.1, ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
CC -!- FUNCTION: NADPH-dependent reductase which is a central component of the
CC cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
CC Transfers electrons from NADPH via its FAD and FMN prosthetic groups to
CC the [2Fe-2S] cluster of DRE2, another key component of the CIA
CC machinery. In turn, this reduced cluster provides electrons for
CC assembly of cytosolic iron-sulfur cluster proteins. Positively controls
CC H(2)O(2)-induced cell death. {ECO:0000256|HAMAP-Rule:MF_03178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [2Fe-2S]-[protein] = H(+) + NADP(+) + 2
CC reduced [2Fe-2S]-[protein]; Xref=Rhea:RHEA:67716, Rhea:RHEA-
CC COMP:17327, Rhea:RHEA-COMP:17328, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000256|HAMAP-Rule:MF_03178};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_03178};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|HAMAP-Rule:MF_03178};
CC -!- SUBUNIT: Interacts with DRE2; as part of the cytosolic iron-sulfur (Fe-
CC S) protein assembly (CIA) machinery. {ECO:0000256|HAMAP-Rule:MF_03178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03178}.
CC Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03178}. Note=Relocalizes to
CC mitochondria after H(2)O(2) exposure. {ECO:0000256|HAMAP-
CC Rule:MF_03178}.
CC -!- SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase
CC NDOR1 family. {ECO:0000256|HAMAP-Rule:MF_03178}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000256|HAMAP-
CC Rule:MF_03178}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC family. {ECO:0000256|HAMAP-Rule:MF_03178}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03178}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HF679024; CCT64360.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DPI7; -.
DR STRING; 1279085.S0DPI7; -.
DR EnsemblFungi; CCT64360; CCT64360; FFUJ_04425.
DR VEuPathDB; FungiDB:FFUJ_04425; -.
DR HOGENOM; CLU_001570_17_6_1; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000016800; Chromosome 2.
DR GO; GO:0097361; C:CIA complex; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_03178; NDOR1; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR028879; NDOR1.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF10; NADPH-DEPENDENT DIFLAVIN OXIDOREDUCTASE 1; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03178};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_03178};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_03178};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_03178};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03178};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03178};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03178}; Reference proteome {ECO:0000313|Proteomes:UP000016800}.
FT DOMAIN 8..152
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 210..457
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 14..19
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 61..64
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 99..108
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 134
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 388..391
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 429..432
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 472
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 528..529
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 534..538
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 598
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
SQ SEQUENCE 603 AA; 68759 MW; 82E299ECF633DD72 CRC64;
MAAHDRSVLV LYGSETGNAQ DMAEELGRIC QRLHFESRVE ELDAVDLNAL LQPDFVLFVI
STTGQGDMPH NSLVFWKRLL RKKLPPGCLA SVKYTTFGLG DSTYVKFNWA ARKLNRRLDQ
LGATTFFDPF EADEQFPDGI DGSFVRWGER LYNHLLEHHP PPTGLEPIPD DVILPPKWSL
KSSLRNSSIS NGHKSPIISN LPPSSPLPIP NGWNATLVGN DRLTPEKHWQ DVRLISFDIP
HRDGDKLSCV PGDCLTIYPK NFPPDVQKLI TLMGWEEVAD KTLDLSLCES LPTNLYIDPK
CTLRELLLNN IDFTAIPRRS FLKNMSYFST NPDHKERLLE FTMTEYLDEY FDYATRSRRS
ILEVLEEFTS VKLPAERLFD IFPIIRGRDF SIANGGEHQN HPTDKDKTRI ELLVALVKYK
TVLRKPREGL CSRYLDNIPL DSILAVTRKP VLSPIHGLQN ARRPLVAIAT GTGLAPIRAL
MHERLTHPSP GPMHLFFGNR NRGADYFFEQ ELDAAVREGH LNVFLAFSRD QRNKIYVQDR
LREEAKRIEE VILNNGIFCV CGGSTKMADA AKKVVFDPFS EDVKDTEERK KILAALTWWQ
EIW
//
