ID A0A0D2EVT1_9EURO Unreviewed; 780 AA.
AC A0A0D2EVT1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-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=PV05_10618 {ECO:0000313|EMBL:KIW51949.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW51949.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW51949.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW51949.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847322; KIW51949.1; -; Genomic_DNA.
DR RefSeq; XP_013312533.1; XM_013457079.1.
DR AlphaFoldDB; A0A0D2EVT1; -.
DR STRING; 348802.A0A0D2EVT1; -.
DR GeneID; 25332526; -.
DR HOGENOM; CLU_010365_7_1_1; -.
DR OrthoDB; 2140484at2759; -.
DR Proteomes; UP000054342; 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; 2.
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:SF23; FERRIC-CHELATE REDUCTASE-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 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:UP000054342};
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 58..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 507..524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 389..500
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 780 AA; 88471 MW; 9E3EE4B779C4B452 CRC64;
MSSMATEALA QLAKREEDSW DRIADGLVKR VNIPINSTTP PALVQAIQQD PFSHAAKYGL
LFVYVGIILL LSATLMRLYY YWGDKIRTAL YKEEVINSAS ATTPMGFSPM HGYVDYELPS
AISAQTDGST RHFFPSKGPL IAEKTRQQAA VSAIAPLNNT IAFFRWIFYR PMPALRIGKF
TFTFPSLGVL VIVTIALLAS LLYCFLPRPL FYASMSYGSP PLAIRAGMMS VSLIPWCVVL
ATKANPVSWM TGIGHDRLIV LHRWTAYLCV IFAIIHAVPY WYQSVNDPDG YATFKLYFNQ
QYYVFTTGIA AIAPLLFLTL HSLPILRAKM YELFVILHIP VAWAFIGLLF WHCNNYLTSW
AYLYSTIALM SVSLFARLVF LNWTNPFRSS WLIGEESAVT ILPENAIKVT IPTQKRWRPG
QYAYLRMPGI SILENHPFTI ASLCSEDFPS QYGEQYRDMT LVFRPFSGFT RKVMDTAIKK
GPYKTYRAFV EGPYGGMQRQ MASFDQVVFF AGGSGITAIA SQLLDLIKRM RDGKATTSKV
HVIWAMKRPD IMEWFKEELR ICRECAPPGS VQCHFYITAS RRYEPLPEVK EHRLGGIRDK
ISDAIHNAGS KRNSAMVMEG EPDLKKELED QITALPQAYL APPRHLSPSS AEQLQTYYPP
PPKEARMSTI SQAQIEATRA FDFGFPQTPT KFQKNLMRFA FLPTNVSSRR DGWRTEYGRP
DIPYMLKGLS KEFGRRTCVY VCGPPEMRTD VTNTVARLQR DIWSDSGKDE IFLHAENYAL
//
