ID I3MN44_ICTTR Unreviewed; 301 AA.
AC I3MN44;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=1,5-anhydro-D-fructose reductase {ECO:0000256|ARBA:ARBA00041155};
DE EC=1.1.1.263 {ECO:0000256|ARBA:ARBA00039066};
DE AltName: Full=Aldo-keto reductase family 1 member C-like protein 2 {ECO:0000256|ARBA:ARBA00043095};
DE AltName: Full=Aldo-keto reductase family 1 member E2 {ECO:0000256|ARBA:ARBA00041996};
GN Name=AKR1E2 {ECO:0000313|Ensembl:ENSSTOP00000013026.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000013026.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000013026.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037014};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC {ECO:0000256|ARBA:ARBA00007905}.
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DR EMBL; AGTP01016942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01016943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005320382.1; XM_005320325.2.
DR AlphaFoldDB; I3MN44; -.
DR STRING; 43179.ENSSTOP00000013026; -.
DR Ensembl; ENSSTOT00000014538.3; ENSSTOP00000013026.3; ENSSTOG00000014534.3.
DR GeneID; 101955263; -.
DR CTD; 83592; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000153272; -.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; I3MN44; -.
DR OrthoDB; 890110at2759; -.
DR TreeFam; TF106492; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 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 PANTHER; PTHR11732:SF391; 1,5-ANHYDRO-D-FRUCTOSE REDUCTASE; 1.
DR PANTHER; PTHR11732; ALDO/KETO REDUCTASE; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT DOMAIN 7..278
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 40
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 69
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 301 AA; 34378 MW; 0D6047D6CC05983E CRC64;
MAKIPAVGLG TWKASPGEAT EAVKVAIDAG YRHFDCAYLY HNENEIGAGI RQKIKEGVVR
REDLFVVSKL WCTYHEPSLV KVACKKSLKA LKLDYLDLYL MHWPMGFQPG EEDVPLDLCG
VVIPSDTSFL KTWEAMEDLV IKGLVKDIGV SNFNHEQLES LLNKPDLKFK PITNQIECHP
YLTQKNLISF CKARDVSVTA YRPLGGSREG TDLLNNPTIR RIANHYNKSC AQILIRFQIQ
RDLIVIPKST NPKRIQENIQ VFDFELTENH MDEIMSLNKN LRLATFPTTE SHKDYPFHID
F
//
