ID I8AAV2_ASPO3 Unreviewed; 710 AA.
AC I8AAV2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=Ao3042_00281 {ECO:0000313|EMBL:EIT82487.1};
OS Aspergillus oryzae (strain 3.042) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1160506 {ECO:0000313|EMBL:EIT82487.1, ECO:0000313|Proteomes:UP000002812};
RN [1] {ECO:0000313|EMBL:EIT82487.1, ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|EMBL:EIT82487.1,
RC ECO:0000313|Proteomes:UP000002812};
RX PubMed=22933657; DOI=10.1128/EC.00160-12;
RA Zhao G., Yao Y., Qi W., Wang C., Hou L., Zeng B., Cao X.;
RT "Draft genome sequence of Aspergillus oryzae strain 3.042.";
RL Eukaryot. Cell 11:1178-1178(2012).
RN [2] {ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|Proteomes:UP000002812};
RA Zhao G., Hou L., Wang C., Cao X.;
RT "Comparative genomic analyses of Aspergillus oryzae 3.042 and A. oryzae
RT RIB40 for soy-sauce fermentation.";
RL Submitted (JUN-2012) 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:EIT82487.1}.
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DR EMBL; AKHY01000076; EIT82487.1; -; Genomic_DNA.
DR AlphaFoldDB; I8AAV2; -.
DR HOGENOM; CLU_010365_6_0_1; -.
DR Proteomes; UP000002812; 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 Gene3D; 2.40.30.10; Translation factors; 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; 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 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 70..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 304..416
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 556..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 79396 MW; 5613C49D0CC85807 CRC64;
MSMGGMDMGP MGHMSMGDGV PGLFYLQKMY WAVVGSAIAA GTVVNAFNNF LAFQRLRDST
LTPSKPKSLF FITCATLTAI VREASYATLP PWSLGGRIIH FAPLGPLAII LANLVVVLVF
CFYKLDTTDQ WKWEDVGYRT GFVAIAQLPL IFLLAGRQNI IGLLVGMSYE RLNWFHRWIS
RTLWLTVTIH MGFWFRSWGR YDYITYQLKN DPLSKRGFAA WCILTFIVLS SMAPIRRLSY
EFFVLQHLVT FVGFIVAVWL HAAEEVKVWV WISIGLLVFD RVARYAWATY ANLSIFHRST
SNTKHALWAN RASFTPLPGN VTRITIDNPG IRWEPGQHVF LTCHSIVPLQ SHPFTIASIS
ADNKMEFFVR SEKGGTRRFF RYASKHHHVL GSRDTSPVKP ARAVFIDGPY GKMRPLRQFD
SVILLAGGMG VTFVIPCLRD IVSRWKMECL GDNEQSKKSP RLTPTKRIRF VWVIKSRAQL
SWFETQLQSV LSDVEECRRA QPDINREIEL SIYVTCDEKL EPQPQPAQPL CSQAQPESTI
VGTRQDANSI ELAAVTDEKR SKKDDVSIHS ISNVSSGDST PQSGCLPNGG CCCTTAIEDE
DNNSITVHNC SCSGHAAASQ APGPEPEKLD VKAAPIKVPE LPMFSGRPQP RTIIRKVLEK
AEGESAVVVC GPQGLSDDVR RSVVYLSDER AVHKGTGAQG IYLHAEKFGW
//
