ID A0A010SGT6_9PEZI Unreviewed; 565 AA.
AC A0A010SGT6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=CFIO01_04863 {ECO:0000313|EMBL:EXF84003.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF84003.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF84003.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF84003.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXF84003.1}.
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DR EMBL; JARH01000213; EXF84003.1; -; Genomic_DNA.
DR RefSeq; XP_007592309.1; XM_007592247.1.
DR AlphaFoldDB; A0A010SGT6; -.
DR KEGG; cfj:CFIO01_04863; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_010365_5_0_1; -.
DR OrthoDB; 1779950at2759; -.
DR Proteomes; UP000020467; 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:UP000020467};
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 26..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 250..365
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 444..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 61937 MW; EA41E0A8B8832F66 CRC64;
MIEPRAAKKP KPPNARQLLN EWNVKVYAGV VAGVIAALII YHWAQWIRRR TSKSPRTGSS
SSLAKASRKI RSLLVRKVPG FPTGGHALLT IAFVGVNIVM SFHNVDKAKM SNFAARFGWM
STANMALCVF FGLKNTPLGV LTGHSYERLN FFHRLAGYAA VLQMLLHAIF YMVYYGTQDR
WSTLLEVQNW EGIGAGFAMV LLLMGLARNL GYEWFYVSHL VGFLLAVIFT GLHRPYWIWK
IPVAMVFIAA IWGLDRLIRG SRMLYNLVNN SATIYRLPDN GVRLVIKKPL SGATPGSHCF
VWIPGVRPFQ THPFTIVSNT PHGGLELVLS SYDGFTKALH DLANTEAGTT VWASVDGPYG
AFPNPKNYDK VVLIAGGSGA TFTFGLATSL LQHLESESHK RVDFIWAVRK RENLEWFTDH
LQSLSQHGAG VNVLLHVTRE GSTASLSESS ENVSSPTSLK SPNEKVEALL PEPGTEQNKE
TLPSTTAVPQ GDGSLGLEGL CDIKFDKLRA GEAINQTLQS AAPGQRVLIA ACGPQSLTEI
VQNAAAHCIA TGDISVEVHC ENFGW
//
