GenomeNet

Database: UniProt
Entry: F2Q038_TRIEC
LinkDB: F2Q038_TRIEC
Original site: F2Q038_TRIEC 
ID   F2Q038_TRIEC            Unreviewed;       616 AA.
AC   F2Q038;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE            EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN   ORFNames=TEQG_06420 {ECO:0000313|EMBL:EGE07506.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(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: 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS995761; EGE07506.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2Q038; -.
DR   VEuPathDB; FungiDB:TEQG_06420; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_010365_6_0_1; -.
DR   Proteomes; UP000009169; 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; 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   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   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        25..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        100..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          298..404
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          505..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  68247 MW;  5C82E0D68FF5C1C2 CRC64;
     MAHNHGGGAT PTGDGVPTYF EMQRMYWAVV GTAIGVATAC NILNKIVAAQ RSTDTTRTPA
     KPKSLFFNIY ATLTAITREY SSATLSPLKM GRWEFQPSPL GRVSVVLANF IAVMVFCFYR
     LDTLDKWSWE TVGYRTGFMT VAQLPLILLL AGKRNIIGFL TGSSHERLNW LHRWTARTLW
     LSATIHMGFW FRSWGRFNYI ATKVRTDPLT QRGIAAWSIL TFILFATLAP VGRWSYELFF
     ISHVVTYAGF IAAAWLHAEP EVKMWVWVSI ALVVFDRVAR SAMMVWSNLA IFSRSSSSSS
     LWANYATFIP LAGDVTRVTV RNPVISWKPG QHVFLSIPAL APFQSHPFTI SSLPSDNKIE
     FLIRAESGAT RAILNHAEKW NTAIDSDSTR LVALDGPYGA IRALRQFDSV VFFAGSMGVT
     FTMPLLRDIV EGWRAGSNGG SLPITKHVHF VWAIRSHSHI SWFQKELESL MRDVEDCRAT
     NPKFKPTFAI SIYLTSDPHM SATSPSAHGT GLYIQRTPST TSDSSQTTTS LSPLVSWEKG
     LSSKSPVCLR TGRPNIDNII LSTLEVAEGE SAVVVCGPSG LSTDVRRNVV SLSDERAVHK
     GTGAQGIYLH VEEFGF
//
DBGET integrated database retrieval system