ID F0XUN0_GROCL Unreviewed; 934 AA.
AC F0XUN0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=CMQ_4593 {ECO:0000313|EMBL:EFW98741.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFW98741.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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; GL630006; EFW98741.1; -; Genomic_DNA.
DR RefSeq; XP_014168224.1; XM_014312749.1.
DR AlphaFoldDB; F0XUN0; -.
DR STRING; 655863.F0XUN0; -.
DR GeneID; 25977821; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_010365_7_1_1; -.
DR InParanoid; F0XUN0; -.
DR OrthoDB; 2140484at2759; -.
DR Proteomes; UP000007796; 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:UP000007796};
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 44..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 541..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 425..540
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 742..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 103181 MW; A78BC08B1D51C489 CRC64;
MATRLQPEAP ALARRINIPL TATSPAGLIE ADTVDPWNKS GKYALAWTYF ALALTGCVVV
VRLWHYWQDK IRQAIYKQEV EEHYRNLYVT NPEWEQPAAT AGSLAEQEAA QAAQAAQAAQ
AAQAAQAAQA AQAAQAAQAA QAAQYAQYAQ YGQHGPNGPN GTPATVSHAS SRHFFPEETK
QETAFRPTGN FSSVGPVNDA IALFRWLFYR PLPDVVWRKY RFTFSSVAVL ACGFVALAFS
ALYCFLPQPL YWQSIRFGAP PVAVRAGMMA VAMTPWIIAT STKTNVLTLI TGIGPERLNV
LHRWAGYLCL FLSLVHAIPF YVQPVWGDGG MAVFQRLFSN GLIVYGTGIA CLVPLIWLCV
ASLPIVRRVA YEAFVLLHVP VGLLYVGLLF WHTKNFLHSW AYLYATCAIF GACQLWRLAK
LNWTRPWRLA FLVGDEAAIS LMAEDAIKIT IPTQMRWQPG QYVYLRMPGI SLFENHPFTV
SSLCSEDFPS AYGDAYRDCV LVFRPYGGFT RRVLDTAVSK GPFHTYRAFL DGPYGGMRRE
LAAFDTCILI AGGSGITSLM SQLLNLIKRM RDGKAITKRI VVVWALRRLE AMDWFREELR
ICRESAPPES VTCKFFVTAA TRAEHRNPHL GGDALGLFGG PDATTSSVVF TPGMGGMGAH
HQQRAPRPLS NLFHDRLDGF VAGIASKRNS ALIVAEAQGD PEVERQLRAE DEDRITALPQ
QKYLQPYQMQ VPLPDESLRR LEGRGEKQAA QATEASQPGE FHFTPHPRTD APHFNLAPPV
LAAREAVGSG EDEGENENET TSEAQMRPPE LAHLRTDSGP TSTFGPPSGF DFGFPETPTE
FQRSLMRFAF PVPHQIDGGW SVEYGRPDLG YMLHEWARGG ADGRGILGRR TAVFVCGPAS
MRVGVATTVA ALQAEIWGDD MLEEIFLHTE NYAL
//
