ID A0A427YAM0_9TREE Unreviewed; 435 AA.
AC A0A427YAM0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-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_000730 {ECO:0000313|EMBL:RSH88199.1};
OS Apiotrichum porosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Apiotrichum.
OX NCBI_TaxID=105984 {ECO:0000313|EMBL:RSH88199.1, ECO:0000313|Proteomes:UP000279236};
RN [1] {ECO:0000313|EMBL:RSH88199.1, ECO:0000313|Proteomes:UP000279236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27194 {ECO:0000313|EMBL:RSH88199.1,
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 -!- 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 eukaryotic ribosomal protein eL22 family.
CC {ECO:0000256|ARBA:ARBA00007817}.
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:RSH88199.1}.
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DR EMBL; RSCE01000001; RSH88199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427YAM0; -.
DR STRING; 105984.A0A427YAM0; -.
DR OrthoDB; 2879766at2759; -.
DR Proteomes; UP000279236; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006826; P:iron ion transport; IEA:UniProt.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.30.1360.210; -; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR002671; Ribosomal_eL22.
DR InterPro; IPR038526; Ribosomal_eL22_sf.
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; PF01776; Ribosomal_L22e; 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 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 51..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..318
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 435 AA; 49042 MW; 8513ADA2245E8F4F CRC64;
MEGPAQAVMT AQQIPNAADL PQQPNNPAPY PGGVKPKKYH WYAMVGGNQG VANQMGVMAF
SQLPLIILLI MKNNPISFLT GISYQKLNYL HRAASRACLI CSWTHAIAWT PRVLAKGHFD
HAYIIWGLVA LFSFTMLWTT SFRLVRRVAW EFFILAHIVF SILFLVGAII HWQRKKLWVW
PSVALGLWAV DRLIRLCRLV ISNFCTGRRL NGDSVALREQ NLVELLDGNV LRVTIRRRSF
RWSAGQHAFL SFTSVTSSPH ESHPFSLANI PSGSDNSAVF LIRVHSGATK LLRDVLVQPR
ETSIPIFIEG PYGAPKATSS SKTAGKALHK FYVDYSVPAN DNVFDPAAFE KFLHDRIKVD
GKPGQLGDVI QISKEGNKLV LSSQIPFSKR YLKYLTKKHL KKNSFENFLR VVATSKDTYS
LRYFKVDQDE AEDEE
//