AIM14_PICST
ID AIM14_PICST Reviewed; 524 AA.
AC A3LN69;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Probable metalloreductase AIM14;
DE EC=1.16.1.-;
GN Name=AIM14; Synonyms=FRE3.1; ORFNames=PICST_87040;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- FUNCTION: Probable cell surface metalloreductase. May be involved in
CC iron or copper homeostasis (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family. AIM14
CC subfamily. {ECO:0000305}.
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DR EMBL; CP000496; ABN64279.2; -; Genomic_DNA.
DR RefSeq; XP_001382308.2; XM_001382271.1.
DR AlphaFoldDB; A3LN69; -.
DR SMR; A3LN69; -.
DR STRING; 4924.XP_001382308.2; -.
DR EnsemblFungi; ABN64279; ABN64279; PICST_87040.
DR GeneID; 4836723; -.
DR KEGG; pic:PICST_87040; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_036508_0_0_1; -.
DR InParanoid; A3LN69; -.
DR OMA; LIPLHKW; -.
DR OrthoDB; 936110at2759; -.
DR Proteomes; UP000002258; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR013112; FAD-bd_8.
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.
PE 3: Inferred from homology;
KW Electron transport; FAD; Flavoprotein; Ion transport; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..524
FT /note="Probable metalloreductase AIM14"
FT /id="PRO_0000408748"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 105..222
FT /note="Ferric oxidoreductase"
FT DOMAIN 248..372
FT /note="FAD-binding FR-type"
SQ SEQUENCE 524 AA; 59993 MW; 1E3A7D060BD22377 CRC64;
MSWYSVDSEI ESLERRHAGH HHTVNIKYGY VILALSIVHM VLSISGKKLY FKNWAETGRA
SSWWRSVVSI PFWVSTLVWL AIFAFLSIFH IEELSENYTT AVKRLGRMAY CLVPFTIFIS
LRPPNTVGYQ SGYYLEKLNL HKWISRLIFA TAIGHGLGFL YKWTKEGALA EKIFKFDNFL
GVTVFALMPV LIFASVNVMR RRNYRLFYIL HNVTLWMFVV LIAFHARPGV PLLAVINLAL
LGYQIYQRFF KSYYLHDISV VESPYSKMQI IRIPRPETFP SYLPGSHIRL GYSATNISAW
LYATHPFTIA STNDDSESTL DLVMNKPVNF PIDITSPYTM TGPFPSLPPQ FYTTARHVNI
ICGGSGISFG LPIYKYFVNS NRSIPIRLIW CIRSSDDTFI LDHLLPERSI DVQIYITSNT
GSLNQQQSAS TIFDEEADAL LEGDSTTNIE MANLATDKEE KKTDHFNTIH DGRPNFDDAF
GNLAAAVDVD EKWLIACGPR KLIDDCRKWT KGKDIEFYSE LYEM