ID A0A427XEJ5_9TREE Unreviewed; 1053 AA.
AC A0A427XEJ5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=EHS24_003483 {ECO:0000313|EMBL:RSH77183.1};
OS Apiotrichum porosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Apiotrichum.
OX NCBI_TaxID=105984 {ECO:0000313|EMBL:RSH77183.1, ECO:0000313|Proteomes:UP000279236};
RN [1] {ECO:0000313|EMBL:RSH77183.1, ECO:0000313|Proteomes:UP000279236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27194 {ECO:0000313|EMBL:RSH77183.1,
RC ECO:0000313|Proteomes:UP000279236};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Apiotrichum porosum DSM 27194.";
RL Submitted (NOV-2018) 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:RSH77183.1}.
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DR EMBL; RSCE01000017; RSH77183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427XEJ5; -.
DR STRING; 105984.A0A427XEJ5; -.
DR OrthoDB; 1461913at2759; -.
DR Proteomes; UP000279236; 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; 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:UP000279236};
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 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 470..589
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 673..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..841
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 115594 MW; D84F3C3C7405C7E0 CRC64;
MSTSTTSTAV ATTAIKILSS TIRSTGTAVS TATSKALSSE SLSKAATTTT AKVASVAKAV
SSSTPGSLSS TSLVKVITTS SSKLSTTLAT TSTLTTTSTG PSAAAAATSS ILSSMTSAAS
AVETVETAIP SGKKAFAWAY IHAHQSLTTD PTYRYAYLFW ILVGALAIVY AIAHHFRLSG
GWLGAWYNKW GMKRGTVRYG PKKSGRYFVL PSNSYLVTMG VFVFIMLMLL LAGPDHIEES
KGVWEMRRSL SDLKRSLEEV EIIKPLHKEH VDKSVWTLGN RFGFMAFAAM PLIVVLALKS
TPFALFTIPW FTALHWDKVG TFHRAGGWFV WWMVTLHVIL WVIQLFKDHY DNRPMFFAML
VIYRFRSAIV AYVAMTLAML LSLRKVRNKS YELFYFSHVI LMFIMLVFAL LHHAVIWYWI
GAALMLWGGD RVFRWTRGAW INGSFGSSQA IKSANPRLDA YMEKNGAPVP SIVPPGMAHA
QLLPSRTVRL SIRTARPIKW QPGQSVLLNI PDLSLLQTHP FTISNNDPHE MVLVIKARKG
LTRQLYDHVV AMTNAQVNSH DKRGSVIFRT EPVLMRAQID GPLGSAGRVP WTDFSNVVIM
CGGSGVTFGL AICDYLATVM SSPQFKGKTR RVRFVWIVRE YAEITWAASA MCRFAHLLQG
EQLQIDIFVT NGEKSTRPQR KRTPATSMIS VQSPADADDS ESSDDDDDGK AAGTNTGNNL
RPPRPSYYEL PGRERKASTD TVSSAFSVTP RSSQERVTSD IDPETGAAYN DEAAIRGLTN
YGDEEDVDDA KEKRLSRAFQ HEGKARRARS RRAARAASMP GAVLPPVPPM PDPATMPPPP
SPPKLMVDIS ADLERDERRR SQKPHMQTEE SRSIVATDSS ATLRDTYGRL TGESGIPIVS
YNDNTWAAYE RYDPFGETGK LSPGASLEDL ALHYKSLTSR THDMVLLDDT PDGAGHKCDH
CGRAASDQLW IDEGDYAAAK ILSENARTGR PPLASILEDE MRSATGSTIV ATCGPVGLNT
TVRNLVSAAI DPAKIRNGDP RGYVTMYSED FEM
//
