ID N1P6D1_YEASC Unreviewed; 712 AA.
AC N1P6D1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=CENPK1137D_440 {ECO:0000313|EMBL:EIW08670.1};
OS Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=889517 {ECO:0000313|EMBL:EIW08670.1};
RN [1] {ECO:0000313|EMBL:EIW08670.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CEN.PK113-7D {ECO:0000313|EMBL:EIW08670.1};
RA Nijkamp J.F., van den Broek M.A., Datema E., de Kok S., Bosman L.,
RA Luttink M.A., Daran-Lapujade P., Vongsangnak W., Nielsen J., Heijne W.H.M.,
RA Klaassen P., Platt D., Paddon C.J., Koetter P., van Ham R.C.,
RA Reinders M.J.T., Pronk J.T., de Ridder D., Daran J.-M.;
RT "De novo sequencing, assembly and analysis of the genome of the laboratory
RT strain Saccharomyces cerevisiae CEN.PK113-7D, a model for modern industrial
RT biotechnology.";
RL Submitted (MAR-2012) 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; CM001533; EIW08670.1; -; Genomic_DNA.
DR AlphaFoldDB; N1P6D1; -.
DR SMR; N1P6D1; -.
DR HOGENOM; CLU_010365_4_0_1; -.
DR Proteomes; UP000013192; Chromosome XII.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0000041; P:transition metal 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 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 PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|ARBA:ARBA00022617};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Iron {ECO:0000256|ARBA:ARBA00022617};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|SAM:SignalP};
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:ARBA00022448}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..712
FT /note="ferric-chelate reductase (NADPH)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004109592"
FT TRANSMEM 170..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 412..546
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 712 AA; 81989 MW; 5224F12B51544BAA CRC64;
MHRTLLFLTW LISLTKAFNI KLPHTEKKDH LESNAVLACA SYINTLKWSF DSSVVPGFYS
TICSYSPAFD TWSLCIFNSL TDQIIPMDNT SFEESLGNVR KTCSFVDKKF SNISLEQYYS
SLNNASSHAL EDYGSIESLS TSIRVDRETR SRWIRAFHAH AYNLDISSVY GAYLTYYFVI
VGIIAVFFHM SHYNGLNRAL FASRFVNYIR GHFVLPTFLV DKHANHFKFL NVEVFTGLMP
NSLEAWIIFG YTLANIIFLS ISYIIDPYNL IFNSHLSQFT RLLADRSGIL AFTQFPLIII
FTARNSFLEF LTGVKFNSFI SFHKWIGRIM VLNATIHSLS YSLFAIINHA FKISNKQLYW
KFGIASITVL CVLLVLSLGI VRKRHYEFFL YTHIILALLF FYCCWQHVKI FNGWKEWIVV
SLLIWGLEKL FRIWNILQFR FPKATLINLN TSNNPHDEMF KVIIPKYNRR WHSKPGQYCF
IYFLHPLVFW QCHPFTIIDE GEKCVLVIKP KSGLTRFIYN HILQSLNGKL QLRVAIEGPY
GPSNLHLDKF DHLLLLSGGT GLPGPLDHAI KLSRNPDKPK SIDLIMAIKN PSFLNGYKSE
ILELKNSRSH VNVQVYLTQK TAVTKAANAR DQLIHFDDIM TELTSFAHIG NARPNFSNVI
ENAIKSTPPG DSLAVVCCGP PVLVDDVRNT VSQKLLGYPE RIIEYFEEYQ CW
//
