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Database: UniProt
Entry: A0A395GJW0_9EURO
LinkDB: A0A395GJW0_9EURO
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ID   A0A395GJW0_9EURO        Unreviewed;       608 AA.
AC   A0A395GJW0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE            EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN   ORFNames=BO80DRAFT_250586 {ECO:0000313|EMBL:RAK95749.1};
OS   Aspergillus ibericus CBS 121593.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK95749.1, ECO:0000313|Proteomes:UP000249402};
RN   [1] {ECO:0000313|EMBL:RAK95749.1, ECO:0000313|Proteomes:UP000249402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK95749.1,
RC   ECO:0000313|Proteomes:UP000249402};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC       {ECO:0000256|ARBA:ARBA00006278}.
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DR   EMBL; KZ824486; RAK95749.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395GJW0; -.
DR   STRING; 1448316.A0A395GJW0; -.
DR   VEuPathDB; FungiDB:BO80DRAFT_250586; -.
DR   OrthoDB; 2787294at2759; -.
DR   Proteomes; UP000249402; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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:SF27; FAD-BINDING FR-TYPE DOMAIN-CONTAINING PROTEIN-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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000249402};
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        20..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        221..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          301..429
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   608 AA;  68295 MW;  080F80C3E8448183 CRC64;
     MGVDHLQPGE ERQIDYHPPM NVALATPMFI LAGAFFVLFV GRSLIRLHHR RRLHQILQTD
     SQEKFERSSA LSASLNKHVF YAPLLSVRHS RYFRLGENIH MGIIPLRLEA VLLTAYILIN
     IVFFFVLVDW GKDWDEVVFQ FQYSAGSMAV LNLPALVLAA GRNNPLVPLL GIKFDCFNLM
     HRWVGRTIIM AGLVHTISAV VMKEHEEGGL AAATKLIWNT KFFICGLVAI FAFATILLQS
     TSPVRHAFYE AFLHTHILLA IMAFVGLWYH LEGMSQQNAL LVTLVLWGFD RATRLACVIW
     RNVGKHRTKA TVELLPGDVA RVNVSLARPW SFQAGQYMYL YMPSLGLWTS HPFSVAWTAT
     GETGLAEKRS SQDSTNRLVG ESQQTTMSFL IKRRDGFTSR LLRKVCTSTE RRFSAIALAE
     GPFGGLESLN SYGTVLLVAG GIGITHPMSY IYEFVNKFAS RSTAVRRVTL VWVVRSLDHL
     SWIQPWMASL FHHPALQDAS VPKQESYFEV PDFSLSIQVY LSTRECSPED YSPAESPWAI
     AAPSRVPISI NSGKPCFREL LELEMAQQVG AMAVSVCGPG ALGDDLRQVV REKQGVKKVD
     LYEETFSW
//
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