FREB_ASPFU
ID FREB_ASPFU Reviewed; 743 AA.
AC Q4WR75;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ferric/cupric reductase transmembrane component B {ECO:0000250|UniProtKB:P32791};
DE EC=1.-.-.- {ECO:0000305|PubMed:21840411};
DE AltName: Full=Ferric reductase B {ECO:0000303|PubMed:21840411};
DE Short=Ferrireductase B {ECO:0000303|PubMed:21840411};
DE AltName: Full=Ferric-chelate reductase B {ECO:0000250|UniProtKB:P32791};
DE AltName: Full=Metalloreductase freB {ECO:0000303|PubMed:21840411};
DE Flags: Precursor;
GN Name=freB {ECO:0000303|PubMed:21840411};
GN Synonyms=fre2 {ECO:0000303|PubMed:21062375}; ORFNames=AFUA_1G17270;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP INDUCTION.
RX PubMed=21062375; DOI=10.1111/j.1365-2958.2010.07389.x;
RA Liu H., Gravelat F.N., Chiang L.Y., Chen D., Vanier G., Ejzykowicz D.E.,
RA Ibrahim A.S., Nierman W.C., Sheppard D.C., Filler S.G.;
RT "Aspergillus fumigatus AcuM regulates both iron acquisition and
RT gluconeogenesis.";
RL Mol. Microbiol. 78:1038-1054(2010).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21840411; DOI=10.1016/j.fgb.2011.07.009;
RA Blatzer M., Binder U., Haas H.;
RT "The metalloreductase FreB is involved in adaptation of Aspergillus
RT fumigatus to iron starvation.";
RL Fungal Genet. Biol. 48:1027-1033(2011).
CC -!- FUNCTION: Ferric reductase involved in adaptation to iron starvation
CC and which is most likely part of the reductive iron assimilatory system
CC (RIA), a siderophore-independent high affinity iron uptake mechanism
CC (PubMed:21840411). {ECO:0000269|PubMed:21840411}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P32791};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P32791};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P36033};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is repressed by iron in a sreA- and acuM-mediated
CC way (PubMed:21062375, PubMed:21840411). {ECO:0000269|PubMed:21062375,
CC ECO:0000269|PubMed:21840411}.
CC -!- DISRUPTION PHENOTYPE: Reduces ferrireductase activity and decreases
CC biomass production during iron starvation but not during iron and
CC copper sufficiency and copper starvation (PubMed:21840411). Increases
CC sensitivity to hydrogen peroxide (PubMed:21840411).
CC {ECO:0000269|PubMed:21840411}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000004; EAL91057.2; -; Genomic_DNA.
DR RefSeq; XP_753095.2; XM_748002.2.
DR AlphaFoldDB; Q4WR75; -.
DR SMR; Q4WR75; -.
DR STRING; 746128.CADAFUBP00001634; -.
DR EnsemblFungi; EAL91057; EAL91057; AFUA_1G17270.
DR GeneID; 3510127; -.
DR KEGG; afm:AFUA_1G17270; -.
DR VEuPathDB; FungiDB:Afu1g17270; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_010365_1_0_1; -.
DR InParanoid; Q4WR75; -.
DR OMA; RWTGYES; -.
DR OrthoDB; 1506659at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
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:0000293; F:ferric-chelate reductase activity; IMP:AspGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IGI:AspGD.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IMP:AspGD.
DR GO; GO:0015677; P:copper ion import; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR Gene3D; 3.40.50.80; -; 1.
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; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Ion transport; Iron; Iron transport; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..743
FT /note="Ferric/cupric reductase transmembrane component B"
FT /evidence="ECO:0000255"
FT /id="PRO_5004246419"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 273..389
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000255"
FT DOMAIN 411..590
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 503..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 309
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P32791"
FT BINDING 323
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P32791"
FT BINDING 379
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P32791"
FT BINDING 393
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P32791"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 743 AA; 84747 MW; 9EBEC3446D4E30CD CRC64;
MLLVSCLIIL LHLQNALSQI IPPNERCVTA VYTAYEYLSF SGQPNKGLWA PRCRNRLHVL
SIYAASDLYC SDAEREAGFA QLDDQCRQYA GVDLIPRQEF APNLTHEAIS QMRVVEFGEL
PKKGPLDTPI LISKSYYSRV FRTIDAWQFE LWSHYAFGYL GYAYWTVVIA AGALHKLVLH
AISVKRAPSL PPFPFLLLIY YWIQTNLIIP APLASSRRRL LWWTFPGRIH AIVVLLFWIL
SIVLCLIGYR TFSDNIYWPD ISAQLLRYVA DRTGILSFAN VPLLWLFAGR NNIFIWATGW
SYSTFNIFHR HVAWIATLQA VVHTILYTVL FIQSGNAWKK MQKPYLLWGT LAMLAMILVF
PFAVDWFRRR TYETFLVLHI LFSVVALVGC FYHVIIFEDH EYWFYLWPAV VIWVSDRVLR
LIRIVYCNLH VQLGSRSRFQ CTECVAAYDK DADIIHLELT PGSGLQPAPG QYYFLYQPFR
LTGWESHPFT LGYWSYNDGA PSTQCRSLKR DTTTDVSEIP LLPDTPSSGS DYGSIDTSTD
PPERKLALRF WIRPYDGWTR HLRDQCLQSP TRIIQPNILL EGPYGEQCPL WKYESVLLIA
GGTGIAAAVP YIQDHILRSS TGQTSTQSIH LVWTARQPAL LRDIAGRELK QALSRKDFRV
SFYVTSESAS QGAIMDGVEF ACGRPDLQAI ITAHAEEARL GSSSVLVLVC GPSGMAGLAR
AAVHQAMRWG CRSLRYVEES FDW
