FRE8_ASHGO
ID FRE8_ASHGO Reviewed; 686 AA.
AC Q75CQ8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable ferric reductase transmembrane component;
DE EC=1.16.1.7;
DE AltName: Full=Ferric-chelate reductase 8;
GN Name=FRE8; OrderedLocusNames=ACL139W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Is required for the uptake of Fe(3+) ions. May participate in
CC the transport of electrons from cytoplasm to an extracellular substrate
CC (Fe(3+) ion) via FAD and heme intermediates. Involved in iron
CC homeostasis (By similarity). {ECO:0000250}.
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; Multi-pass membrane protein.
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DR EMBL; AE016816; AAS51089.1; -; Genomic_DNA.
DR RefSeq; NP_983265.1; NM_208618.1.
DR AlphaFoldDB; Q75CQ8; -.
DR STRING; 33169.AAS51089; -.
DR PRIDE; Q75CQ8; -.
DR EnsemblFungi; AAS51089; AAS51089; AGOS_ACL139W.
DR GeneID; 4619385; -.
DR KEGG; ago:AGOS_ACL139W; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_025685_0_0_1; -.
DR InParanoid; Q75CQ8; -.
DR OMA; LLPIHKW; -.
DR Proteomes; UP000000591; Chromosome III.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0140618; F:ferric-chelate reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR Pfam; PF01794; Ferric_reduct; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
PE 3: Inferred from homology;
KW Electron transport; FAD; Flavoprotein; Glycoprotein; Ion transport; Iron;
KW Iron transport; Membrane; NAD; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..686
FT /note="Probable ferric reductase transmembrane component"
FT /id="PRO_0000239646"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 108..666
FT /note="Ferric oxidoreductase"
FT BINDING 308..314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 431..439
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 686 AA; 77515 MW; 0700CDD72C5E2E91 CRC64;
MGGAWQEAVV RSIGAADERM VRLSGWASLA LALGLVCVVV PVVNYMRLNP WVFRVMHHWR
HHVMRRHGAM CRKLVQQRTL WLALLWCMLG GACAVVGSAD VVVVTKRLGR VAAAFMPALF
LLTLRPSPLP YTLYLSLLPM HKWLGRVVVL QATVHSALYT WYFATSGKMA KMKKTANWMG
AVALLAFVLI AATSLPAVRR RRFRTFYYVH YVGTWVSVLA VHVHSRPPVT TYTVLNVALL
LYQAWYRISR MSTTTVTVVP ISTSLALLEF PLADLVEKPQ LPSGHVRINL RAPSILGRVF
QHIMPMQHPF TVASLPTDTT VRLIVRKSRF PLVNNGKYYV TGAFEPKVDF LSHRKRRMPG
SWAPEPASPF QCQSPSLQSS PLHYNIKASR VLMVVGGSAI SFGLPFLRIL NFNGVNVRLI
WVCRDYHDLR ILSQFRSNFN GLEIYVTGTN CEEQDLNIDY VDYDERSSEG ERDPERCALL
SPKASEYNCL TPTTGGSTLS GRDAHNYSTF QNRCHSCKHL DRGCRDLEDH AIADINDEID
FTDFFSTRHS TSKYHPKENS KLPVITKDSV FRKPNYVVPP VFDRYDLKTG FTTYTTREKL
SIPTGVKLFF GRPVLSPRDY HWCLQKECIG PSETNECCRA DIANSTHVDD LARVWVLAAG
PQALVEATRI WASDGGLHFH EESFKV
