FREL_CANAX
ID FREL_CANAX Reviewed; 669 AA.
AC P78588;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Probable ferric reductase transmembrane component;
DE EC=1.16.1.7;
DE AltName: Full=Ferric-chelate reductase;
GN Name=CFL1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060 / 2024;
RX PubMed=8828219; DOI=10.1099/00221287-142-9-2515;
RA Yamada-Okabe T., Shimmi O., Doi R., Mizumoto K., Arisawa M.,
RA Yamada-Okabe H.;
RT "Isolation of the mRNA-capping enzyme and ferric-reductase-related genes
RT from Candida albicans.";
RL Microbiology 142:2515-2523(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-
CC siderophore + NADH; Xref=Rhea:RHEA:15061, Rhea:RHEA-COMP:11342,
CC Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.16.1.7;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
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DR EMBL; D83181; BAA11834.1; -; Genomic_DNA.
DR AlphaFoldDB; P78588; -.
DR SMR; P78588; -.
DR VEuPathDB; FungiDB:C4_05770C_A; -.
DR VEuPathDB; FungiDB:CAWG_03246; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140618; F:ferric-chelate reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0000041; P:transition metal ion transport; IEA:UniProt.
DR Gene3D; 3.40.50.80; -; 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 Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Electron transport; FAD; Flavoprotein; Glycoprotein; Ion transport; Iron;
KW Iron transport; Membrane; NAD; Oxidoreductase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..669
FT /note="Probable ferric reductase transmembrane component"
FT /id="PRO_0000210151"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 239..373
FT /note="Ferric oxidoreductase"
FT DOMAIN 374..492
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 17..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437..442
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 669 AA; 74748 MW; E3373CF93EAC2A83 CRC64;
MTESKFHAKY DKIQAEFKTN GTEYAKMTTK SSSGSKTSTS ASKSSKSTGS SNASKSSTNA
HGSNSSTSST SSSSSKSGKG NSGTSTTETI TTPLLIDYKK FTPYKDAYQM SNNNFNLSIN
YGSGLLGYWA GILAIAIFAN MIKKMFPSLT NNLSGSISNL FRKHLFLPAT FRKKKAQEFS
IGVYGFFDGL IPTRLETIIV VIFVVLTGLF SALHIHHVKD NPQYATKNAE LGHLIADRTG
ILGTFLIPLL ILFGGRNNFL QWLTGWDFAT FIMYHRWISR VDVLLIIVHA ITFSVSDKAT
GKYKNRMKRD FMIWGTVSTI CGGFILFQAM LFFRRKCYEV FFLIHIVLVV FFVVGGYYHL
ESQGYGDFMW AAIAVWAFDR VVRLGRIFFF GARKATVSIK GDDTLKIEVP KPKYWKSVAG
GHAFIHFLKP TLFLQSHPFT FTTTESNDKI VLYAKIKNGI TSNIAKYLSP LPGNTATIRV
LVEGPYGEPS SAGRNCKNVV FVAGGNGIPG IYSECVDLAK KSKNQSIKLI WIIRHWKSLS
WFTEELEYLK KTNVQSTIYV TQPQDCSGLE CFEHDVSFEK KSDEKDSVES SQYSLISNIK
QGLSHVEFIE GRPDISTQVE QEVKQADGAI GFVTCGHPAM VDELRFAVTQ NLNVSKHRVE
YHEQLQTWA
