ID G7X9V2_ASPKW Unreviewed; 798 AA.
AC G7X9V2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=FRE family ferric-chelate reductase {ECO:0000313|EMBL:GAA84154.1};
GN ORFNames=AKAW_02269 {ECO:0000313|EMBL:GAA84154.1};
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:GAA84154.1};
RN [1] {ECO:0000313|EMBL:GAA84154.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA84154.1};
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}.
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DR EMBL; DF126450; GAA84154.1; -; Genomic_DNA.
DR AlphaFoldDB; G7X9V2; -.
DR STRING; 1033177.G7X9V2; -.
DR VEuPathDB; FungiDB:AKAW_02269; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; G7X9V2; -.
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:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
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; 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:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..798
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003505361"
FT TRANSMEM 156..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 445..607
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 532..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 90975 MW; 6C9E80B0494E170C CRC64;
MLSTSWLLLL VYLGLACAGR PPTDEGCVTA VYTALGYLSF SGDPTQGAWE ARCQNRLKVT
STYASADVYC TEEEQVAGFA QLQRYCLEYG KVELMPREQV AENLTHDALS RMPVIEYGQI
PKSQRIPTAV LISPTFYRRT FDTIDTWQFE VWSHNVFGLL GYAFWALVLA VGIFHRLVRH
IFHALDIRAG QWARSRVRWL WIPLDGTYHW LQTHLVVPAP LPSSRRKLLW WTFPTRIEAV
TVLLFWVLSV VVCTLEYRPV EGNLYWPSIP DQIMRYAADR TGVLSFANLP LVWLFAGRNN
IFIWATGWSF GTFNLFHRHV AWIATVQAVA HTLIYLVIMY QKGNVIRKLH KPYLIWGTLA
TVVMVAILPL AVQWFRHRVY ETFLLLHILC SIAVLFGCFY HTIIFEGHDY WNYLWPAVAI
WIVDRSLRLI RLIYCNIHVR ANAGKGVQYT RSTATYDPSS DVIRLEVTPG SAHIRPSPGD
FYYLYQPFRL TGWESHPFTL GAWSYDTHNR KSASTKDNEV DIDVTQVPLL SDPFSPGTAT
PDETQLKHPQ KHSHNRHVQQ QIPKFIFWIR PYDGWTRSLR QQCINSPNLT TTTTILLEGP
YGNHFPLWSY ESVLLIAGGT GIAAAVPYIQ DHVVRSSTES EQILSSSRKD GNTTQTKDMR
LIWVTRQEAF AQQVAGRELV PALARDDFRA EFYCTSSSTP APPRSVGHDD DDDGSDTDTD
RRSSRDHLWK GGSGNINFLP GRPNLESLVL DHAHEAQLSE SSAVVLVCGP SALADEARAA
VHLAMRRGYR RIRYVESW
//
