ID Q0UZN5_PHANO Unreviewed; 627 AA.
AC Q0UZN5;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=SNOG_02779 {ECO:0000313|EMBL:EAT89510.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT89510.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-
CC siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342,
CC Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000496};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000256|ARBA:ARBA00006278}.
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DR EMBL; CH445328; EAT89510.1; -; Genomic_DNA.
DR RefSeq; XP_001793375.1; XM_001793323.1.
DR AlphaFoldDB; Q0UZN5; -.
DR EnsemblFungi; SNOT_02779; SNOT_02779; SNOG_02779.
DR GeneID; 5970232; -.
DR KEGG; pno:SNOG_02779; -.
DR VEuPathDB; FungiDB:JI435_027790; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_010365_7_2_1; -.
DR InParanoid; Q0UZN5; -.
DR OMA; LVFYIRH; -.
DR OrthoDB; 1776577at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR32361:SF23; FERRIC-CHELATE REDUCTASE-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00023065}.
FT DOMAIN 297..408
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 627 AA; 70626 MW; 9F0D5F715678E947 CRC64;
MAGWLSAPLQ LHSMRMFECG KKTPEECDWY KHHWHFWYIA DYVFALPTIA FFMCTIGVFI
IGHAVSSLSG YRRVRGPRIW GKTIAVVRYL SYRGFYVKAL RWNSAPVGVL LLGLIGTIFF
FCMDLAPKPY YWPDIKFGGS PPLATRSGWL ALACMPFVFA TATKTNWITL CTGVSHERLQ
VFHRWISYAF FILALLHTFP FIVYHIHWHD MEDHFASSLL FYWTGIVALI FQAWLTFMSH
STIRRFGYEF FKATHIFAAV VFVVTFFWHC DYTLTSWDYF IATAAVYVPC YVYPWLRTCF
EYGVTQKASI SVDGSGFIRV VIPTKAAWKP GQHCFLRFTS LGLRHAISSH PFTICSLPSM
QTNKSNELVF YIRPHGGFTA TLYAYALEHP GSLVSVLVDG PYGGIYLQTY TNVDHLLVVA
GGSGAAWCLP FVEQFVRYGV PRQDARLAHK ENVHVEIGSE TGGLVRPMSL RLILATRNNT
NRTWFIGAVN KILDKYETTE SSSNVHVEVY LTGDAAKEAE LSNKGLEDAL TPSGSSSAGD
EIGIPKHDQG GTAPRPVFEG RPQLPSIIKE EAEKVREERE SLGVYVCGPT TMQNDVRNAV
AAENLNILSG SSRAGGVYLH SEHFSWA
//
