AIM14_PICGU
ID AIM14_PICGU Reviewed; 482 AA.
AC A5DE11;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Probable metalloreductase AIM14;
DE EC=1.16.1.-;
GN Name=AIM14; ORFNames=PGUG_01512;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408156; EDK37414.2; -; Genomic_DNA.
DR RefSeq; XP_001485841.1; XM_001485791.1.
DR AlphaFoldDB; A5DE11; -.
DR SMR; A5DE11; -.
DR STRING; 4929.XP_001485841.1; -.
DR EnsemblFungi; EDK37414; EDK37414; PGUG_01512.
DR GeneID; 5127468; -.
DR KEGG; pgu:PGUG_01512; -.
DR VEuPathDB; FungiDB:PGUG_01512; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_036508_0_0_1; -.
DR InParanoid; A5DE11; -.
DR OMA; LIPLHKW; -.
DR OrthoDB; 936110at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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..482
FT /note="Probable metalloreductase AIM14"
FT /id="PRO_0000408747"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 86..198
FT /note="Ferric oxidoreductase"
FT DOMAIN 225..348
FT /note="FAD-binding FR-type"
SQ SEQUENCE 482 AA; 54837 MW; D4A8B874DBD4D2FF CRC64;
MHNHPRHEGH LHTVNVKYGY VVFLLSIVHI VVVATVPRLR KVGSSSTRRS LPWLPQIVIW
AILLAILGVW NIHEWSEHYN VSIKRFGRMA YCLLPFDILL AYKYWPLENY LQNLNLHKWM
SRIIVVCSMI HGIGYFVKWF VEGTFFHHLF KIDNLLGVVV FAAAVVLLVV SVALFRRQSY
RLFYVSHNIT IGMFVVLILF HARPPVTLFV AICGLLLAIL FFIKFQTYSA TPVSLKEVPN
SSLVLVSFPW PDHIATSFKP GSHVRINHSN RSWKSWVFAS HPFTSATLPG TSETLDLVVK
KGTFIFAKDT QYNLSSPYTS LSFDDNSISR FDQSVIICGG SGISLAIPVF KYLITKLDVT
MIWCTRSKAD LFVLRHYSLL DKVQVYITGN DSLSVEDESE GHGLMHETIE LENLEESSKN
SEATKQPEIL RGRPDLNNVC ASLETTPNSS CVISCGPRSL VKDCENWCRN HKIESVTEIY
EM