ID A0A401KYX9_ASPAW Unreviewed; 600 AA.
AC A0A401KYX9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=AAWM_07391 {ECO:0000313|EMBL:GCB24506.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB24506.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB24506.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB24506.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) 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: 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:GCB24506.1}.
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DR EMBL; BDHI01000021; GCB24506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KYX9; -.
DR STRING; 105351.A0A401KYX9; -.
DR Proteomes; UP000286921; 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:UP000286921};
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 16..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 292..447
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 600 AA; 68030 MW; E3A8EE17EA044ADC CRC64;
MDSNLWYAML NDTLCYANLW VLACMIVVVF AWQSSGRLSA HLRRLASFTD HRQTYHRIPN
FHVAWLKRHL LDAPLLRSRH NQEWQLSRAV NMGTLPSRFH TLLLTVIVVM NVVLCTNTVP
YGSKESTVAE LIRNRTGYMA TANLFPLLVM AGRNNPLIPL LRVSFDTWNL LHRWLGRIVV
LEGLAHVIAW GVPKVQTYGW STALGTLKKP FMFNGLMGIV AMLFILVQSP SPIRHAFYET
FLHLHIGLAC VSVGFLWHHV YRYSCRYYLY AAVAFWAFER LARLLILIYR NYGFGRRTTA
YLEALPGDAV RVTLQLARPW TFSPGQYCFV YIPKLGAWTS HPFSIAWGET GQTLLGSYSE
KMAEVELGND HGQPGLESRK VNTVSLLVRR RTGFTDKLFT EAFAYARTRL PPDTISTSPR
STTTDISTAA MPVTAFVEGP YGNLHSLDSY GTVLLFAGGV GITHCLPFIR HLVQGYSDGT
VAARRVTLVW VIQSPEHLDW IRPWMTTILG MEGRRDVLRI QLFVTRPRNP REIRSPSATV
QMFPGRPDVG TLVQMEIENQ VGAMGVMVCG NGGLSDDVRR ACRQRQGRTQ LDYIEESFTW
//
