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Database: UniProt
Entry: S3CGK2_OPHP1
LinkDB: S3CGK2_OPHP1
Original site: S3CGK2_OPHP1 
ID   S3CGK2_OPHP1            Unreviewed;       643 AA.
AC   S3CGK2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE            EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN   ORFNames=F503_02157 {ECO:0000313|EMBL:EPE05418.1};
OS   Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX   NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE05418.1, ECO:0000313|Proteomes:UP000016923};
RN   [1] {ECO:0000313|EMBL:EPE05418.1, ECO:0000313|Proteomes:UP000016923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE05418.1,
RC   ECO:0000313|Proteomes:UP000016923};
RX   PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA   Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA   Robertson G., Birol I., Bohlmann J., Breuil C.;
RT   "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT   a comparison with the bark beetle-associated pine pathogen Grosmannia
RT   clavigera.";
RL   BMC Genomics 14:373-373(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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC       {ECO:0000256|ARBA:ARBA00006278}.
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DR   EMBL; KE148156; EPE05418.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3CGK2; -.
DR   STRING; 1262450.S3CGK2; -.
DR   VEuPathDB; FungiDB:F503_02157; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_010365_6_0_1; -.
DR   OMA; GFRNAWV; -.
DR   OrthoDB; 1385919at2759; -.
DR   Proteomes; UP000016923; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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   Gene3D; 2.40.30.10; Translation factors; 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; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000016923};
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        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        143..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        173..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        211..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        237..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          291..411
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          505..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   643 AA;  70609 MW;  5D1BBC5F78E0B6A6 CRC64;
     MDMSMGANMF QTPNMALARI YWYLVAAVVA LFVAVRAVNY YDSSIRLRTS ASASYAYPTK
     PRTPFLQSWA TATAVAREIT YPQFFVSVPY LSWLTPPPAG RLIILLVYWA VILGFMCAGA
     IVHDVNFYER IGFRNAWVTV TQLPLLYLLA GKTSVIASLT GTSHERLNWM HRWIARTMFV
     TASVHGWHFY TEYRKAGLAS YFFEVMPMGK YGIAAWGLLL WSFVVGVAPI RHLCYEVFVI
     QHIATACLLL WAVHKHVPSY AEYNVWFAVA ALGFDRVVRF LMLVFQNIKL ATPDRARCKG
     GRRIGHDAQV RAVGDDIAIV TIKDVHFTWR AGQHLYLWIP ALGPLEHHPY TIACAHVLPE
     TCVCNSVQLV VRKHGGFSKR LHDRAAKDQA AAKKTTLTAF VTGPFGEPAR WDIYETLVLI
     SASTGASFTL PILESVLQAA ADDTRGGKKK AICTKRIDFL LSAKKGDEIG YYVGRLHELL
     DKAKTVGIEL SVSIAVTRDK SPLVGMAPSA QSHNVPQSGL SDSYSSSSSV DKTAKVATTT
     ITPGEQSSAC CMATPDAEKT AAGLRKVASN DSHVQQLATR PDIAAFVRNA VETTGGETSV
     VVCGGKSLVA RTRNCVAQLS DERAVHKGTG AQGIHLHVEE YGF
//
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