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Database: UniProt
Entry: A0A194S5Z4_RHOGW
LinkDB: A0A194S5Z4_RHOGW
Original site: A0A194S5Z4_RHOGW 
ID   A0A194S5Z4_RHOGW        Unreviewed;       633 AA.
AC   A0A194S5Z4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE            EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN   ORFNames=RHOBADRAFT_52194 {ECO:0000313|EMBL:KPV76148.1};
OS   Rhodotorula graminis (strain WP1).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV76148.1, ECO:0000313|Proteomes:UP000053890};
RN   [1] {ECO:0000313|EMBL:KPV76148.1, ECO:0000313|Proteomes:UP000053890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:KPV76148.1,
RC   ECO:0000313|Proteomes:UP000053890};
RX   PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA   Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA   Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT   "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT   graminis WP1.";
RL   Front. Microbiol. 6:978-978(2015).
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; KQ474076; KPV76148.1; -; Genomic_DNA.
DR   RefSeq; XP_018272197.1; XM_018416220.1.
DR   AlphaFoldDB; A0A194S5Z4; -.
DR   STRING; 578459.A0A194S5Z4; -.
DR   GeneID; 28976668; -.
DR   OMA; WVYILAT; -.
DR   OrthoDB; 2052724at2759; -.
DR   Proteomes; UP000053890; 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: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:UP000053890};
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        70..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          292..456
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   633 AA;  67416 MW;  32991C7A4CD60A1F CRC64;
     MSAHADLNRF ARHVVAVEQV TELAKRAASA AANATSADGG AGAAAAAAAK KAAMLDQTTW
     NDAVRQDFNI VLGFAAALAL LACAPAAASW FANGRYASGW MLRRGSSTAS EVHVGSREKE
     SGDKGGEKFS TVEVVERPLP VKITPTSALF ASTRTIYNRT LLLTSPLFGL TWGQVVVCLL
     YELLFTFVLF YHCLDHRTNW RRSAGVALAQ LPAVFILATK NNALSLLGKG YEKLNYLHRV
     AGRLTILGGL LHTLFFLLMA PLDVKKPVHA SGLVCTVASV LIFITSLSYF RNRWYQVFLV
     SHVAGWVSLL VALNFHVPQL ARPYTAFVLV CYGTDLACRL VKTRFGSASV ASLPGGTVMV
     QSHSLKTGWR AGQHVWVRVP SAAGLLRGWE THPFTIANAP AECSPLDGSH ALTLLAKSTG
     SWTRSLEAHA RSTAGPNEAR VIKCAVEGPY GGLMFTDFID SSAVILVAGG SGITFCASVL
     EELVYLATQG RTSTRSATLV WTVKDLAQLE SYQSFLTGLV DVARDKTCLN LRVLLHVTRP
     PLGTPSFGTL ASPVPQSVLS IGRPSLPAIL DVVAAEVMAS VQRRGLVRGA GIVVGACGPK
     PLVRDVREVV GAVQEGKAVA VGGIVCHTES FGW
//
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