ID A0A2H1A606_CANAR Unreviewed; 659 AA.
AC A0A2H1A606;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=B9J08_000782 {ECO:0000313|EMBL:PIS58288.1}, CA7LBN_002347
GN {ECO:0000313|EMBL:QWW23546.1};
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS58288.1, ECO:0000313|Proteomes:UP000230249};
RN [1] {ECO:0000313|EMBL:PIS58288.1, ECO:0000313|Proteomes:UP000230249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS58288.1,
RC ECO:0000313|Proteomes:UP000230249};
RX PubMed=27988485; DOI=.1093/cid/ciw691;
RA Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT continents confirmed by whole-genome sequencing and epidemiological
RT analyses.";
RL Clin. Infect. Dis. 64:134-140(2017).
RN [2] {ECO:0000313|EMBL:PIS58288.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS58288.1};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida auris genome assembly and annotation.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QWW23546.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA7LBN {ECO:0000313|EMBL:QWW23546.1};
RA Finianos M.;
RT "Candida auris outbreak in lebanese hospital.";
RL Submitted (JUN-2021) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; PEKT02000002; PIS58288.1; -; Genomic_DNA.
DR EMBL; CP076750; QWW23546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H1A606; -.
DR EnsemblFungi; B9J08_000782-t37_1; B9J08_000782-t37_1-p1; B9J08_000782.
DR VEuPathDB; FungiDB:B9J08_000782; -.
DR VEuPathDB; FungiDB:CJI96_0003316; -.
DR VEuPathDB; FungiDB:CJI97_000783; -.
DR VEuPathDB; FungiDB:CJJ07_000619; -.
DR VEuPathDB; FungiDB:CJJ09_002742; -.
DR VEuPathDB; FungiDB:QG37_08067; -.
DR OMA; IRNNPFI; -.
DR OrthoDB; 2787294at2759; -.
DR Proteomes; UP000230249; Unassembled WGS sequence.
DR Proteomes; UP000825438; Chromosome II.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR PANTHER; PTHR32361:SF25; FERRIC_CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT 1; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 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 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
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:UP000230249};
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:ARBA00023065}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..659
FT /note="ferric-chelate reductase (NADPH)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033759034"
FT TRANSMEM 155..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 394..513
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 659 AA; 75896 MW; 4C7A2CE096843DE7 CRC64;
MLFSRYLGIL LLISQAQSLV IVDSSIASAC IYYMKQFDWG CGGTGQGHKY YSCRCGNVDW
LGSVASCISG QTNNKGKIDH ALKHVTTRCL QKGHFHYTVD DMKQWRENAT KYIEQPTAHD
IKERVYHPLG VNQTDFAVYM RSFDEINHHV FKSQWLGWGL LYYWVAVVVI FAMLHLSQIY
LGLRPPRRIA QFCEKYLTPV RLWGYSFLDI VVMGLFLVFT VLATALSYTV QLPNVYMNDV
YFLTLDLIGY RSAIISFSLL PVVFIFGLRN NPFTFLTGLP RATFIKYHNY VAIIMSIEAL
IHSAVWTDYA INEAGYSAWS IDDYWRWGIV GTVLLFIMIG QSFQPVRNFM YEAFLVIHIV
FGWLFIVAMW YHCVTLGWMG WVYTMIALTV YDRVMRWAKI LVLNRGLTEL YVTVVDERTL
ELTLPKPLAY DMSYRPGSSV YVTFLHSKIW SQCLQSHPFS IISSPATSSN VLKMYVRVKR
GATRSLLRLP ADEKGRLRLW CLLDGPYGGF TYKHRDSDDR VYIAGGLGVC SLLPHVYSNP
AGAKLIWTVA NAREFWCMRR DINYVRERGT EVTVYVRDPS GIELDDEKMS FVQPADRRPD
FDELIGEHVK AAKADKKRDL CIYSCGPGNM DRQIKQIATR QIEVGSDFSV HHKSMNYQW
//
