ID   AKCL2_RAT               Reviewed;         301 AA.
AC   Q5U1Y4;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=1,5-anhydro-D-fructose reductase;
DE            Short=AF reductase;
DE            EC=1.1.1.263 {ECO:0000250|UniProtKB:Q9DCT1};
DE   AltName: Full=Aldo-keto reductase family 1 member C-like protein 2;
DE   AltName: Full=Aldo-keto reductase family 1 member E2;
GN   Name=Akr1e2; Synonyms=Akr1cl2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-
CC       fructose (AF) to 1,5-anhydro-D-glucitol.
CC       {ECO:0000250|UniProtKB:Q9DCT1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,5-anhydro-D-glucitol + NADP(+) = 1,5-anhydro-D-fructose +
CC         H(+) + NADPH; Xref=Rhea:RHEA:20665, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16070, ChEBI:CHEBI:16715, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.263;
CC         Evidence={ECO:0000250|UniProtKB:Q9DCT1};
CC   -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoic acid and
CC       alkyliodines. {ECO:0000250|UniProtKB:P82125}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P82125}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; BC086397; AAH86397.1; -; mRNA.
DR   RefSeq; NP_001008343.1; NM_001008342.1.
DR   AlphaFoldDB; Q5U1Y4; -.
DR   SMR; Q5U1Y4; -.
DR   STRING; 10116.ENSRNOP00000023133; -.
DR   jPOST; Q5U1Y4; -.
DR   PaxDb; Q5U1Y4; -.
DR   PRIDE; Q5U1Y4; -.
DR   Ensembl; ENSRNOT00000023133; ENSRNOP00000023133; ENSRNOG00000017165.
DR   GeneID; 307091; -.
DR   KEGG; rno:307091; -.
DR   UCSC; RGD:1309599; rat.
DR   CTD; 83592; -.
DR   RGD; 1309599; Akr1e2.
DR   eggNOG; KOG1577; Eukaryota.
DR   GeneTree; ENSGT00940000153272; -.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   InParanoid; Q5U1Y4; -.
DR   OMA; AEMYANE; -.
DR   OrthoDB; 1016440at2759; -.
DR   PhylomeDB; Q5U1Y4; -.
DR   TreeFam; TF106492; -.
DR   PRO; PR:Q5U1Y4; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   Bgee; ENSRNOG00000017165; Expressed in liver and 20 other tissues.
DR   Genevisible; Q5U1Y4; RN.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0050571; F:1,5-anhydro-D-fructose reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; ISO:RGD.
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.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..301
FT                   /note="1,5-anhydro-D-fructose reductase"
FT                   /id="PRO_0000376896"
FT   ACT_SITE        40
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O60218"
FT   BINDING         35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O60218"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O60218"
FT   BINDING         175
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O60218"
FT   BINDING         246..258
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O60218"
FT   SITE            69
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250|UniProtKB:P14550"
SQ   SEQUENCE   301 AA;  34500 MW;  F6786B806D5AE64B CRC64;
     MHQIPTVGLG TWKASPGEVT DAVKVAINLG YRHFDCAYLY HNESEVGMGI KEKIKEGVVK
     RDELFIVSKL WCTYHKQSLV KTACINTLEA LNLDYLDLYL IHWPMGFKPG DKDIPLDRSG
     KVIPSHTSFL DTWEAMEDLV IEGLVKNIGV SNFNHEQLDR LLNKPGLRIK PITNQIECHP
     YLNQKSLIDF CHGRNVSVTA YRPLGGSRDG VHLMDDIVIR KIAKKHGKSP AQILIRFQIQ
     RNLIVIPKSV NPSRIRENIQ VFDFELTEKD MEELLSLDKN LRLATFPSTE NHKDYPFHIE
     Y