ID A0A1B9GJY9_9TREE Unreviewed; 767 AA.
AC A0A1B9GJY9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=I316_07051 {ECO:0000313|EMBL:OCF31265.1};
OS Kwoniella heveanensis BCC8398.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296120 {ECO:0000313|EMBL:OCF31265.1, ECO:0000313|Proteomes:UP000092666};
RN [1] {ECO:0000313|EMBL:OCF31265.1, ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|EMBL:OCF31265.1,
RC ECO:0000313|Proteomes:UP000092666};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus heveanensis BCC8398.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|Proteomes:UP000092666};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) 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}.
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DR EMBL; KV700136; OCF31265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B9GJY9; -.
DR STRING; 1296120.A0A1B9GJY9; -.
DR Proteomes; UP000092666; 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: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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000092666};
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 109..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 430..535
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..181
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 86573 MW; 9DEB74B47CDEC5AD CRC64;
MADQNHDRNQ QQVFAMADPD PTTSGAIESG PSSSPSTSTS IYSSTALAQE SYPYSYIASS
SSSSSSSSTA TSSGVLSPSH GNVTREMEEE WARQRAISRK VKHDAMRNAW IWIGATFLLL
VLMHLYRQIK HSRRRRRAIR AYDDSQAYKP VSTAHDDLAD DVDEDDEPDT NGNEGPGEGE
GEDEQLVAGL GRSRAGQSRQ SPQIISGKER GRVRRLITGI GATYRNTVYL RSFPWWLYGP
ETVMDALFTI VYTVVYGYLC VAKTEVWFPT KHNTTANQLG VMSFSQLPII LLLVSKNNPI
SNLTGITYQK LNYLHRASSR VCLFTSWLHA LLWTPKVWSA GDTRPYLLFG IAALTGFTML
WVTSFRIIRR MAYEFFLVSH ILFSLLYLIG AFFHWWRMWY WVAPAMAIWA LDRFIRFAKV
MYQNNFHKPN RWKTLGESKI ELLDHDVMRV SIRRDNFYWK AGQHGFISSP SISSSPHESH
PFSIANVPTE SSNEAVFLIR VHSGFTKRMR TALSSDQSNS IPLYLEGPYG YAHNLDSYST
VLLVSGGTGV TFVLGHFLQI LASVRAGMSA VKKLHLVWHI RHAEDIEWIA PLLNQGLLDP
PDSMNIVIDV FVTKSHASDE PWPPEMDLNL TETLHHEIPR LLHLRNEDNY NNNRGSWDEG
CRTCSPNTPM TESRDENLFL PKRATILGRY GLMADAAEKI RWRRGRADLK KIVEEDAGAC
VGCMNVSVCG PTQLLHATKK AVREASNYES SMRGLTSIDF FEETLGA
//
