ID M7T6Q1_EUTLA Unreviewed; 731 AA.
AC M7T6Q1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=UCREL1_10736 {ECO:0000313|EMBL:EMR62335.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR62335.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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; KB707447; EMR62335.1; -; Genomic_DNA.
DR RefSeq; XP_007798575.1; XM_007800384.1.
DR AlphaFoldDB; M7T6Q1; -.
DR STRING; 1287681.M7T6Q1; -.
DR KEGG; ela:UCREL1_10736; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_010365_7_1_1; -.
DR OMA; RWAGYLC; -.
DR OrthoDB; 2140484at2759; -.
DR Proteomes; UP000012174; 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:SF23; FERRIC-CHELATE REDUCTASE-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 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:UP000012174};
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 54..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 483..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 368..482
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 636..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 82892 MW; ECF1D8AAA40BCEC3 CRC64;
MDAAPQPFLA RAATTLTGLV KRIHIPLTTT SPPGLVEANT LDPWDESGKY GLGWTYFAVA
LVGVVIFVRI WHWWQDKIRQ AIYKQEVEQH YRDLYSLDPE FAVTAMQTGQ ASQHFFPDEG
GEKRDFKPKS DLSAVGPVLD ALALFRWVFY RPVPDIVWRK HRFTFSSLAV LALGFIALAF
VSLFVFLKQP LYWQSIQYGS PPVAVRSGMI AVAMTPWIVA TSMKANLLTL ITGIGPERLN
VFHRWAGYLC LFLSLIHTIP FYVQPVWDDG GLEVFSRLFP EGSGIIYGTG VACLVPLVWL
CVASLPVVRR MAYEVFVTLH VPVGIVYLGV LFWHTKNYLG SWNYLWTTVA IWVLCYAMRL
FKLNWLKPWR LSFMVGDEAA ITLMTENAIK ITVPTQMKWK PGQYVYLRMP GISFFDNHPF
TISSLCSDDF PSEYGEQYRD CILVFKPYGG FTRRVLDTAI QKGPFHTYRA YLDGPYGGMR
RELAAFDTCI LIAGGSGITA LMSQLLNLIK RMRDGKAITK KVVVIWALKR LEAMDWFREE
LRICRDSAPP ESVTCKFFVT AAVRQSRVPQ QRERGPRPLS NAFHDRLDGF VAGIASKRNS
AMIRDEAQGN PDYEQQLRAE DEDRITALPQ QKYLQPHAVP PQAPPPVNRQ SAQEESLRRL
EGREETTEGE YDEAPAAPTA DYPEDKPKRE FHFPPLHTRP DLQPHFNYAP PSPRKLPPNS
TSSNDNTPAA A
//
