ID Q0UKH1_PHANO Unreviewed; 823 AA.
AC Q0UKH1;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=SNOG_07743 {ECO:0000313|EMBL:EAT85209.1};
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:EAT85209.1, 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; CH445335; EAT85209.1; -; Genomic_DNA.
DR RefSeq; XP_001798074.1; XM_001798022.1.
DR AlphaFoldDB; Q0UKH1; -.
DR EnsemblFungi; SNOT_07743; SNOT_07743; SNOG_07743.
DR GeneID; 5974967; -.
DR KEGG; pno:SNOG_07743; -.
DR VEuPathDB; FungiDB:JI435_077430; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_010365_7_1_1; -.
DR InParanoid; Q0UKH1; -.
DR OMA; RWAGYLC; -.
DR OrthoDB; 2140484at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase 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; 2.
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 376..490
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 823 AA; 92549 MW; 82CC3F71DFF73C3C CRC64;
MPALRDAMVE QAGVALEQLG EAVSTLTRRV NIPFNSTSPA GLIEANTVDP FNKSGKYALA
YVYFCIPLLV FAALMRYYHL FTDKIRTALH QEEVLQSSTT SSPDTDYEMS VLYTDKSTMK
FFPREGPLPS GPKTQSSVSS VGPINNMVAF FRFIFYRPIR QINIRKGWRP IVFPSLSVTV
IVVAALLVGV LYSCLPQPLF WKSIAYGSPP LAVRSGMMAV ALLPWIVALS MKANFITMIT
GIGHERLNVL HRWAAYICLV LSIMHTVPFY VTPIWEKGAR KSFESLFKQT GFYAYGTGIA
ALVPLAFLCL HSIGPLRHRM YELFVTLHVP VAIVFLGMMF WHCNNYLTSW HYLFSTLTIW
LLSYFVRLFY LNWTRPGRLS WLIGDEAAVT LMPENAIKIT IPTQVRWRPG QYIYLRMPGI
SVFENHPFTI ASLCDEDFPS EYGEGYRDMV IVFRPFGGFT NKVRQAALEH GPWHTYRAFV
DGPYGGMQRR IEAFDDVVLI AGGSGITAII SQLLTLIKKM RDGKAVTRKI HVIWALKRPE
TMEWFKEELR ICREFAPPET VECQFYITAA KRNPAGALVS AKTPTRPVSM FFHDKVNDAF
QNIADHRLSG ISTQRHSALI RDEAQGDPEK ESALRRENED SITALPQAHV LPVNRAHLAP
PRPSFQSHHS DTSNQTDPDM IAPAPRGLAA RRSERSLQLD ISQAVSSGSG AINPNVSESG
AVQGFDFGFP STPTEFQKNL MRFAFLPAAV KKKDGWSTEY GRPDIPYLLK GMSKSFGRRT
CVFVCGPPTM RVSVSDTVAE LQRSVWSNSD RDEIFLHAEN YAL
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