ID   AKCL2_MACFA             Reviewed;         320 AA.
AC   Q4R802;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 70.
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; ORFNames=QtsA-13895;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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; AB168659; BAE00770.1; -; mRNA.
DR   RefSeq; NP_001270572.1; NM_001283643.1.
DR   AlphaFoldDB; Q4R802; -.
DR   SMR; Q4R802; -.
DR   STRING; 9541.XP_005564587.1; -.
DR   GeneID; 101925198; -.
DR   CTD; 83592; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050571; F:1,5-anhydro-D-fructose reductase activity; IEA:UniProtKB-EC.
DR   CDD; cd19110; AKR_AKR1E1-2; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044484; AKR1E2.
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; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..320
FT                   /note="1,5-anhydro-D-fructose reductase"
FT                   /id="PRO_0000287881"
FT   ACT_SITE        40
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O60218"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O60218"
FT   BINDING         194
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O60218"
FT   BINDING         265..277
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   320 AA;  36418 MW;  5D7D2F96E3FBD662 CRC64;
     MGDIPAVGLS CWKASPGKVT EAVKVAIDAG YRHFNCAYFY HNEKEVGAGI RYKIKEGAVR
     REDLFIASKL WCTCHKKSLV KTACRRSLKA LKLNYLDLYL IHWPMGFKPP HPEWIMSCSE
     LSFCLSHPGV HDLPLDESDM VIPGDTDFLD TWEAMEDLVI TGLVKNIGVS NFNHEQLERL
     LNKPGLRFKP VTNQIECHPY LTQKNLISFC QSRGVSVTAY RPLGGSCEGV DLIDDPVIQR
     IAKEHSKSPA QILIRFQTQR NVIVIPGSIT PSHIKENIQV FDFELTQHDM DNILSLDRNL
     RLATFPITKN HKDYPFHIEY