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Database: UniProt
Entry: A0A0G4KV59_9PEZI
LinkDB: A0A0G4KV59_9PEZI
Original site: A0A0G4KV59_9PEZI 
ID   A0A0G4KV59_9PEZI        Unreviewed;       461 AA.
AC   A0A0G4KV59;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE            EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN   ORFNames=BN1708_010869 {ECO:0000313|EMBL:CRK13576.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK13576.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK13576.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK13576.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) 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};
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DR   EMBL; CVQH01004780; CRK13576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4KV59; -.
DR   STRING; 100787.A0A0G4KV59; -.
DR   OrthoDB; 2787294at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR034751; Yippee.
DR   InterPro; IPR004910; Yippee/Mis18/Cereblon.
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; PF08030; NAD_binding_6; 1.
DR   Pfam; PF03226; Yippee-Mis18; 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.
DR   PROSITE; PS51792; YIPPEE; 1.
PE   4: Predicted;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   TRANSMEM        134..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..110
FT                   /note="Yippee"
FT                   /evidence="ECO:0000259|PROSITE:PS51792"
FT   DOMAIN          170..308
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   461 AA;  52394 MW;  68AA96AE8D80AF6E CRC64;
     MGLAYNTYLN SSKIYGCKTC KAHLANHEDI ISRNFRGQHG KAYLFNNVVN IDMGEPSERN
     MTTGRHIVRD ITCRQCKETV GWKYDKAYET TEKYKEGKFI LEAELLCNGT CGFAAIFIQA
     WSPIRHAFYE IFKLLHIALA ILAVMGTWYH LHLKDLPQLR YLIAAIVIWA VDRLWRVFRV
     IYGNFGRGGS RALVEALPGN AVRVTVNMAR PWTFRPGQHA YMYMPSLSYL QSHPFSVAWS
     EDAEDPSSEK LTMNRQDILE MRKTTMSFVI RGRTGFTNTL FQKASACPRG QMHTTCMIEG
     PYGELHSMKS YGTVMLFAGG VGITQAVPHV RDLVIGYANG TVATRRITLV WVIQSPEHLE
     WIRPWMTQIL AMDKRRDVLR IMLFVSRPRS SKEIHSPSAT VQMFPGRPNI DTLLAAEMEQ
     QVGAMGVTVC GPGVLSDDVR RAVRARQYDG EIDFVEEAFS W
//
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