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Database: UniProt
Entry: A0A3M9Y5G0_9PEZI
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Original site: A0A3M9Y5G0_9PEZI 
ID   A0A3M9Y5G0_9PEZI        Unreviewed;       582 AA.
AC   A0A3M9Y5G0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE            EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN   ORFNames=D7B24_008855 {ECO:0000313|EMBL:RNJ55242.1};
OS   Verticillium nonalfalfae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ55242.1, ECO:0000313|Proteomes:UP000267145};
RN   [1] {ECO:0000313|EMBL:RNJ55242.1, ECO:0000313|Proteomes:UP000267145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ55242.1,
RC   ECO:0000313|Proteomes:UP000267145};
RA   Stajich J.E., Kasson M.T.;
RT   "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL   Submitted (OCT-2018) 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:RNJ55242.1}.
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DR   EMBL; RBVV01000082; RNJ55242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M9Y5G0; -.
DR   STRING; 1051616.A0A3M9Y5G0; -.
DR   OrthoDB; 2787294at2759; -.
DR   Proteomes; UP000267145; 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   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        28..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          291..429
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   582 AA;  65449 MW;  4B73C9AE2BAA8229 CRC64;
     MAGPGKDSPE AIAAKAAASA LNASLSNYLY YVMTGCSIVL IAWRLSTQLH RYVRTVACLK
     NDSQRYFAEA STKLSFFKKN VMYAPIFSKR HNREFQLSSA VNVGTLPTRL QLVFLFGYFA
     SNVAFSVIDI PFAATYDDAA RAFRNRTGVL AVVNMIPLFL MAARNNPLIN LLGISFDTFN
     LLHRWFGRIV ILEAIAHTMA FMSAQAHSKS WEAGFQTVLA VPSFFWGFLG TCGFCAIFIQ
     AWSPIRHAFY EIFKLLHIAL AILAVMGTWY HLHLKDLPQL RYLIAAIVIW AVDRLWRVFR
     VIYGNFGRGG SQALVEALPG NAVRVTVNMA RPWTFRPGQH AYMYMPSLSY LQSHPFSVAW
     SEDAEDLSSE KLTMNRQDIL EMRKTTMSFV IRGRTGFTNT LFQKASACPR GQMHTTCMVE
     GPYGELHNMK SYGTVMLFAG GVGITQAVPH VRDLVIGYAN GTVATRRITL VWVIQSPEHL
     EWIRPWMTQI LAMDKRRDVL RIMLFVSRPR SSKEIHSPSA TVQMFPGRPN IDTLLAAEME
     QQIGALGVTV CGPGVLSDDV RRAVRARQYD GEIDFVEEAF SW
//
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