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Database: UniProt
Entry: A0A0H1BE91_9EURO
LinkDB: A0A0H1BE91_9EURO
Original site: A0A0H1BE91_9EURO 
ID   A0A0H1BE91_9EURO        Unreviewed;       598 AA.
AC   A0A0H1BE91;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE            EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN   ORFNames=EMPG_15148 {ECO:0000313|EMBL:KLJ09438.1};
OS   Blastomyces silverae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ09438.1, ECO:0000313|Proteomes:UP000053573};
RN   [1] {ECO:0000313|Proteomes:UP000053573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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}.
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:KLJ09438.1}.
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DR   EMBL; LDEV01002351; KLJ09438.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H1BE91; -.
DR   STRING; 2060906.A0A0H1BE91; -.
DR   OrthoDB; 2787294at2759; -.
DR   Proteomes; UP000053573; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000293; F:ferric-chelate reductase activity; IEA:UniProt.
DR   GO; GO:0006826; P:iron ion transport; IEA:UniProt.
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; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR   PANTHER; PTHR32361:SF24; REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G10820)-RELATED; 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, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053573};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT   TRANSMEM        42..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        202..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        296..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          320..445
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   598 AA;  67454 MW;  587D1BC9D5B6193B CRC64;
     MKSAHILLSV FGTVVVAAHE KRAGGGKHDE GPTEADLLDD RLGRLSLLVG GCALAFFLVW
     HNAIRFSNHL RRLTTLTNDT QRYFTSADPY WAWLKKSVVY APLFRTRHNR EFRLSAAVNV
     GTLPTRFQTF LLFGVIAMNV ALCCVTIPYA SDETTVLGII RNRSGTMATV NLIPLVVMGG
     RNNPLIKLLN VSFDTWNLLH RWFARIVVLE ALTHVIAWMV NKVNTKGWEA VQASFNSQFI
     MTGLIAMIAF LVLALHSPSA LRHAFYETFL HLHQLFVATA FAFLCVHLKS KHALKYIVTA
     IVLWGVERIT RFTLLLYRNF GKKRTTTAVV EVLPGEALRI TLKLVRPWKF KPGQHLYLYV
     PSVGFWMSHP FSAAWSETVD DLTDEKGLVK SRQDVLSTQK SSISLIIRRR TGFTNALFER
     ASATMHGRIS LKAMVEGPYG VDHSLDSYGT VMLFAAGVGI THHVSFVRYL IEGYTQGTVS
     ARRVTLVWII QSPEHLEWIR PWMNTILSME GRRDVLRIML FITRPRNTRE IHSPSSTVQM
     FPGKPNIQTL VDAEIENQIG AMGVLVCGTG SLSDDVRRIC RTRQSGSHID FLEESFSW
//
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