ID E3QPD8_COLGM Unreviewed; 851 AA.
AC E3QPD8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=GLRG_07870 {ECO:0000313|EMBL:EFQ32726.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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; GG697364; EFQ32726.1; -; Genomic_DNA.
DR RefSeq; XP_008096746.1; XM_008098555.1.
DR AlphaFoldDB; E3QPD8; -.
DR STRING; 645133.E3QPD8; -.
DR EnsemblFungi; EFQ32726; EFQ32726; GLRG_07870.
DR GeneID; 24413235; -.
DR VEuPathDB; FungiDB:GLRG_07870; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_010365_7_1_1; -.
DR OrthoDB; 2140484at2759; -.
DR Proteomes; UP000008782; 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; 2.
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:UP000008782};
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 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 482..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 367..481
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 629..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 95899 MW; 809EB3F7647D382B CRC64;
MATRIRDMAD TAGRTAVQLA KRIAITPKPD SPPGLIEALT LDPWAKSGKY GLGWTYFALA
LMGTVLLVRM WHFWQDKIRQ AIYKQEVEEY YANLYNTDPD YAHAVHTGQA QHFFPDSDGL
GEKQFKPRAH FSSVGFVNDT LALFRWMFYR PIPDLAWGSH RFTFSSLAVI TCGLVALAFV
ALYCFLQQPL YWQSIQFGSP PVAIRAGMIA VALTPWIIVT SMKANVLSML IGIGPERLNV
FHRWAGYLCL FLSLVHMIPF YIQPVWDDGG MDVFSRLFPG GSGVIYGTGI ACLVPLVWLC
VASLPFIRRI AYELFVMLHV PVGMAYVGLL FWHTKNYLAS WNYLWATVGI WAFCYFIRLF
NLNWTRPWRL SFMVGDEAAI SLLAENAIKV TIPTQMRWRP GQYVYLRMPG VSFFDNHPFT
ISSLCSDDFP SEYGEQYRDC ILVFKPYGGF TRKVLDMAIE KGPFHTYRAF LDGPYGGMRR
DLAAFDTCIL IAGGSGITAL MSQLLNLIKR MRDGKAITRK VVVVWSLKKL EAMDWFREEL
RICRESAPPE SVTCKFFVTS AVRNRGMAIE GADRGAPRAL SHLFHDKLDG FVAGIASKRN
SALIQSVAQG DVDREQELRA EQEDRITALP QQKYLQPHQY PPPPPGPPPS SRYSAHEQSL
RNLEGRDYDD EDRDAKKREF HFPPINTKGE VPHFNYAPAS PRKVPETSPQ DSDVPVRPPE
LAHLRTTNLP GAGQPRPTST FGPPSGFDFG FPETPTEFQK SLMRFAFPVP HQIDGGWSVE
YGRPDLGYML KEWATGGADG RGILGRRTAV FVCGPPAMRV GVANTVARLQ AAIWGDDMLE
EIYLHTENYA L
//
