ID A0A3D8SJ23_9EURO Unreviewed; 593 AA.
AC A0A3D8SJ23;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=DSM5745_02987 {ECO:0000313|EMBL:RDW86345.1};
OS Aspergillus mulundensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW86345.1, ECO:0000313|Proteomes:UP000256690};
RN [1] {ECO:0000313|EMBL:RDW86345.1, ECO:0000313|Proteomes:UP000256690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW86345.1,
RC ECO:0000313|Proteomes:UP000256690};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW86345.1}.
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DR EMBL; PVWQ01000003; RDW86345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8SJ23; -.
DR STRING; 1810919.A0A3D8SJ23; -.
DR OrthoDB; 2787294at2759; -.
DR Proteomes; UP000256690; 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:UP000256690};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..593
FT /note="ferric-chelate reductase (NADPH)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017720730"
FT TRANSMEM 40..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 303..440
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 593 AA; 66891 MW; 05A158A3C94604F0 CRC64;
MASTLLFMSL VGHSLAADLE RRHGDENPFW GMLNDDYARY SLLALGCFAA SMYIWKMWFR
IAAHMRRLAS FSNERQNYFV PAHKTLARIK KHIVYAPLFR NRHNREFQLS RAVNMGTLPS
RFHTFIIVGI IAMNITLCFV TVPYKSEPES VSGIILSRTG IMATVNLIPL ILLAGRNNPL
ITLLQVPYDT FNLIHRWLAR IVICQALAHT FAWAIPKAQK MGWSGVGQLF GESEFLLSGL
IGTCAFVALL VHSPSAIRHA FYETFLHLHI AFAALSFAYL WIHLDGRNAQ NFLLAAIILW
ALERFARLAI IVYRNIGGRT TTAVVEALPG DAMRITLKLS RPWTFEPGQH MYLYIPAIGW
WTSHPFSIGW SDTEDAMSDE KSLPVSSRDA YGPQTTTVSL LVRRRTGFTD KLFQRAVNAV
DCRVSLTAFA EGPYGSIHSM DSYGSVLLFA GGVGITHLVP FCRHLVKGYA DGTVAARRVT
LIWIIQSPEH LEWIRPWMTS ILAMPRRREV LRIQLFITRP RNTKEIQSPS STVQMFPGRP
NIDTLIGMEV ENQVGALGAL VCGNGSLSDD VRRACRSRQD KTQIDFIEES FTW
//
