ID A2R1R7_ASPNC Unreviewed; 750 AA.
AC A2R1R7;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Contig An13c0070, genomic contig {ECO:0000313|EMBL:CAK41617.1};
DE EC=1.16.1.7 {ECO:0000313|EMBL:CAK41617.1};
GN ORFNames=An13g02180 {ECO:0000313|EMBL:CAK41617.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK41617.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK41617.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270301; CAK41617.1; -; Genomic_DNA.
DR RefSeq; XP_001396356.1; XM_001396319.1.
DR AlphaFoldDB; A2R1R7; -.
DR EnsemblFungi; CAK41617; CAK41617; An13g02180.
DR GeneID; 4986666; -.
DR KEGG; ang:An13g02180; -.
DR VEuPathDB; FungiDB:An13g02180; -.
DR HOGENOM; CLU_010365_1_0_1; -.
DR OrthoDB; 2049651at2759; -.
DR Proteomes; UP000006706; Chromosome 2L.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140618; F:ferric-chelate reductase (NADH) activity; IEA:UniProtKB-EC.
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:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-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 PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
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 ECO:0000313|EMBL:CAK41617.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..750
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002644501"
FT TRANSMEM 178..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 448..585
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 750 AA; 84221 MW; 00CEA442CF28FFDD CRC64;
MLLRISFLAI FVPAMAKQKS FDDAVSSLDA DCLCPIYTAL SQYTFSGTPA GGSYNHSISV
TAFFAEESYI QTLTNFDSIC NSTVEIASMY ASARARCDGN SPAASVSFWQ EVCDVDISSL
ETNRSTTYTS MSIVDPDVNT TASTGTIKNP VLLSESYYRR AYKTCVIHDK ALGQDIRFGW
GLMGYWVAIL VFGMAQKILS LWSARRALDS GRDAEANAVS GPIECKQIPT PLSSISYALR
TYIVVPASFT PIFSHHQRLL YGHSIPKRLD FLIVSGFWIL CVLLACVNYN GAIRTSTMPQ
RNWHYTSDRT GILAYACLPF LWLFTGRNNI FLWATNFDIQ SFSTFHRHIA WACTLLAIVH
SIGYSIILAD YEDAYHEAWS HKPWYMGVIA IIAMSVLLIH SVTWLRRKWY EVFLLSHIIL
AIVIIYALFQ HTRPDGPQWN PYLRTVVAIW MFDRIFRIAR IAYCNLQIRF SELQISLPSS
SVTYNPDSDL IMIDTEAPPH LALKPGQHYF ISQPLSVHCL ESHPFALGAY AQASSRSLKE
KSRLTFYIRP YNGWTKTLRD RCSRAKNTIQ PLLLLEGPYG HTAPLHTFDT VLLIAGGTGI
AATLPYILDY AARLDSQATK TTRLHLIWSA RQRDVFTTVL SDELSHVLQC EGVTISFFCT
GGDPMSPIEI EAIDKEVAIN TTSNIHFCNG RPDIRGAVEN EAEIARECST RLGVLCSGPG
MMADECRLAV YEAMRRGCRG IRYFEEAFTW
//
