ID   ALDR_ENCCU              Reviewed;         301 AA.
AC   Q8SSK6;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Aldose reductase;
DE            Short=AR;
DE            EC=1.1.1.21;
DE   AltName: Full=Aldehyde reductase;
GN   OrderedLocusNames=ECU01_0970;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11157783; DOI=10.1101/gr.164301;
RA   Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA   Weissenbach J., Saurin W., Vivares C.P.;
RT   "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT   parasite Encephalitozoon cuniculi (Microspora).";
RL   Genome Res. 11:198-207(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of
CC       carbonyl-containing compounds to their corresponding alcohols with a
CC       broad range of catalytic efficiencies. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alditol + NAD(+) = an aldose + H(+) + NADH;
CC         Xref=Rhea:RHEA:12785, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.21;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alditol + NADP(+) = an aldose + H(+) + NADPH;
CC         Xref=Rhea:RHEA:12789, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; AL391737; CAD24968.1; -; Genomic_DNA.
DR   RefSeq; XP_965933.1; XM_960840.1.
DR   AlphaFoldDB; Q8SSK6; -.
DR   SMR; Q8SSK6; -.
DR   STRING; 284813.Q8SSK6; -.
DR   GeneID; 860274; -.
DR   KEGG; ecu:ECU01_0970; -.
DR   VEuPathDB; MicrosporidiaDB:ECU01_0970; -.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   InParanoid; Q8SSK6; -.
DR   OMA; WMINDES; -.
DR   OrthoDB; 1016440at2759; -.
DR   Proteomes; UP000000819; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..301
FT                   /note="Aldose reductase"
FT                   /id="PRO_0000381746"
FT   ACT_SITE        51
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         11..20
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         209..266
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  33357 MW;  A682F2EF7E4DE836 CRC64;
     MICKTQKLNN GKEIPTVGLG TWGMEDEAVL EGAIRNALSL GYRHIDTAFI YGNEKMIGNI
     LKKLFDEGVV QRKDLFITSK LWNTFHGCPE DGLRRSLNDL QMDYVDLYLI HWPVTFDPAP
     DGTVESCGKK YNVGKFDAVG VWKKMEALVD LGLAKSIGIS NFGKANTEKI LGTCRICPAA
     IQIELHPYLN QKELVEFMKS KGIQVISYSS LGSAPGSSAK VRDDKTIKAI AKKYGCAPSQ
     IILSYITAQG ICVIPKSRSK EHLRENIDLK ELSREDISAI DALNTGHRYV DPPGFGPEKF
     K