ID A0A0B7F3T3_THACB Unreviewed; 1058 AA.
AC A0A0B7F3T3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-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=RSOLAG1IB_00104 {ECO:0000313|EMBL:CEL51569.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CEL51569.1, ECO:0000313|Proteomes:UP000059188};
RN [1] {ECO:0000313|EMBL:CEL51569.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL51569.1};
RA Wibberg Daniel;
RL Submitted (NOV-2014) 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; LN679100; CEL51569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7F3T3; -.
DR STRING; 1108050.A0A0B7F3T3; -.
DR Proteomes; UP000059188; 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; 2.
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:UP000059188};
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 84..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 518..667
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 764..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 117198 MW; 52A07BD93E17445C CRC64;
MASSTTTPFL PFTDVVPSST ASVVNSYRPP LATGTGGARP ANTASATHYA YGNPNPTTPA
FLSDYQWIAT YLAIHKMSTT TYRYAYMLWL AVTLVAVVVA IAHITGRRTT VLTVIWRKYT
LRRRTWRKQA SLRAIQKSKQ PHRQPYSLPS NAQLIAVIIL FVAAALLCCV GPDYISPWTS
MWDLKANLTS PLLGRRDFMQ AFHDIEKRAP IASTPTTRQP EYTIPKAWWT AGGRTGIIAF
ALFPLCVLFA LKAPPFALFA LPFTTQMHFD KLALLHRWSG RIIWIITTIH VATWGVQLGR
DGRHGKGGIA WDYVWVYPLF IYGIIGYILM TLLVVLSLSP IRTHRYETFY LLHVILVPLT
IIFSALHFPQ IWHWCWVALG LWGGERLFRW ARGAWVNGAV GPWGNFGPVG SVPEPSNLAE
KSADTWEMGV RQSGNNSRST LEDKQPSVRI VSQAPQTNEL LHFFSPTNVQ PSRESVEVNG
GRRERPWSIT SLHTDESVMP RNSFAELIPR NAGNSDSYGP VHTVVSPTRP LVNRSSSTQH
ALVLPPPGFA HCVILPGRTV RLTVVTARPM KWAPGQHVLL CVPSVSQWTT HPFTIAGACD
ERSTGVGARG REISLIIRAR AGFTKLLWEE IMHGSGHHHE HEHGEKPRRG IMLRASIDGP
FGSAARENWT KYSTAIMVAG GSGVAFALSV LEALCLKIVS GEEVKTKRIR FVWMIRDYAH
IQWCAGILRR CREMVPDKDR LQIEIFVTNH QAQTIEVLSS LPSGTEDAML QPPVPRFARD
GRPRPDSVAS NDSLDSTISS NSIAELNPGE HTDGDLGTHV LDYTNFDGEE DTRTAAEATL
SKKVKKEGKL RRARSKKIAV AVSAKLHLEE KRKSMKDFFS HGHGHDDQPL SAPQPRYAQQ
ASGSGSNTPL SATPTGTPRL LSPVNTPKIG GEATLRPPLF VDPTYRSSVA ESMFSRGSVY
DDSRSVFGAD DPVFEMDDEE MEDIYHVAEL ARPGKPKLDK ILADEVERAE GEIVVACCGP
TSLNAAMRKF VADQLSPAKV WRGDMSGSIK LVSEDYAW
//
