ID   FMP46_CANGA             Reviewed;         129 AA.
AC   Q6FJI9;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Putative redox protein FMP46, mitochondrial;
DE            EC=1.-.-.-;
DE   Flags: Precursor;
GN   Name=FMP46; OrderedLocusNames=CAGL0M05951g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Putative mitochondrial redox protein which could be involved
CC       in the reduction of small toxic molecules. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FMP46 family. {ECO:0000305}.
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DR   EMBL; CR380959; CAG62581.1; -; Genomic_DNA.
DR   RefSeq; XP_449605.1; XM_449605.1.
DR   AlphaFoldDB; Q6FJI9; -.
DR   SMR; Q6FJI9; -.
DR   STRING; 5478.XP_449605.1; -.
DR   EnsemblFungi; CAG62581; CAG62581; CAGL0M05951g.
DR   GeneID; 2891653; -.
DR   KEGG; cgr:CAGL0M05951g; -.
DR   CGD; CAL0137471; CAGL0M05951g.
DR   VEuPathDB; FungiDB:CAGL0M05951g; -.
DR   eggNOG; ENOG502S4SU; Eukaryota.
DR   HOGENOM; CLU_1939538_0_0_1; -.
DR   InParanoid; Q6FJI9; -.
DR   OMA; LWVDWEK; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012882; Fmp46.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR28071; PTHR28071; 1.
DR   Pfam; PF07955; DUF1687; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   3: Inferred from homology;
KW   Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..129
FT                   /note="Putative redox protein FMP46, mitochondrial"
FT                   /id="PRO_0000292447"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   129 AA;  15128 MW;  3C5428081C028B33 CRC64;
     MSMFRTLQRQ PRTISLFTHD LENSRPCLSI LEYLKSHTTN RFDLELSTKF PTLDQVHYMN
     AINPMILRAQ IPHLTKIMKL KSYDPLFGSQ LSDCVTKGFW NKEAPLWVDW EKKALGTDLQ
     SIKELLEKD