ID G7XF93_ASPKW Unreviewed; 662 AA.
AC G7XF93;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Ferric-chelate reductase {ECO:0000313|EMBL:GAA85240.1};
GN ORFNames=AKAW_03354 {ECO:0000313|EMBL:GAA85240.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA85240.1};
RN [1] {ECO:0000313|EMBL:GAA85240.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA85240.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DF126453; GAA85240.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XF93; -.
DR STRING; 1033177.G7XF93; -.
DR VEuPathDB; FungiDB:AKAW_03354; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; G7XF93; -.
DR Proteomes; UP000006812; 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:0000041; P:transition metal 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 PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR PANTHER; PTHR32361:SF3; REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13750)-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 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 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 47..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 313..461
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 662 AA; 73953 MW; 9F64B48CB0B3543C CRC64;
MGHIQDFSQD SAMEYHWGYV ARQVPCTKDA GTCAYLDAVY HGHDVSMLYS FILWAVVVGI
LFLWALGGRL VRFDRSVART SPKPVRQSAP YRLSRTIQAL VRRHLLPEAL PWVFGHTTRL
QVLIFLIISG YLLVFTLVGI TYKTWVTPIS GSSLNNTRSG LGPWADRIGV LAFALTPLSI
LLSSRESLLS LITGVPYHHF NFLHRWLGWV IYFQSAMHTI GWTIVEGKLY QPQPAQWNSF
ITQPYIIWGI VAMILLSFLV FHSTKRGIQL TGYEFFRKAH YVVAMVYVGA CWAHWSHLYC
WMLASLVVWF LDRGFRLVRV FVLHHLNVPT TTSSTTGGLH IPHAAIQLHP NPDDGDIIRL
DFHHNHDPWH IGQHFFLCFP QLSLWQAHPL TPCSVPDTLP TGQPHTYIIR ARKGLTRELA
QLARISSQNS QPSDGETTTM TSAGPTTPVI LCGPYGQSIM EETSTAGSSN LLCIAGGTGI
TFVLPPLLHL LSNASTSKSQ PTQILELIWI IRRKADMQWI APELDILQRL ASTHSNTFRV
RIFVTRETAP VPKVSDLEKS PCCAGSSASS DSGVAVQYTL SSEDAAVAGT AAAAHHHPDL
EDIVEDFLDR VVDGPTRVFA SGPAGMITTL RTAVAGRNRP GRVWRGEERW DVQLVHDDRV
EW
//
