ID   S6PD_MALDO              Reviewed;         310 AA.
AC   P28475;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=NADP-dependent D-sorbitol-6-phosphate dehydrogenase;
DE            EC=1.1.1.200;
DE   AltName: Full=Aldose-6-phosphate reductase [NADPH];
DE   AltName: Full=NADP-S6PDH;
GN   Name=S6PDH;
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16653170; DOI=10.1104/pp.100.3.1607;
RA   Kanayama Y., Mori H., Imaseki H., Yamaki S.;
RT   "Nucleotide sequence of a cDNA encoding NADP-sorbitol-6-phosphate
RT   dehydrogenase from apple.";
RL   Plant Physiol. 100:1607-1608(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Greensleeves;
RA   Bains H.S., Tao R., Uratsu S.L., Dandekar A.M.;
RT   "Genomic nucleotide sequence of NADP sorbitol-6-phosphate dehydrogenase
RT   (NADP-S6PDH) gene from apple.";
RL   (er) Plant Gene Register PGR98-193(1998).
CC   -!- FUNCTION: Synthesizes sorbitol-6-phosphate, a key intermediate in the
CC       synthesis of sorbitol which is a major photosynthetic product in many
CC       members of the Rosaceae family.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-sorbitol 6-phosphate + NADP(+) = aldehydo-D-glucose 6-
CC         phosphate + H(+) + NADPH; Xref=Rhea:RHEA:20037, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57584, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:60084; EC=1.1.1.200;
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; D11080; BAA01853.1; -; mRNA.
DR   EMBL; AF057134; AAC97607.1; -; Genomic_DNA.
DR   PIR; T17013; T17013.
DR   RefSeq; NP_001280957.1; NM_001294028.1.
DR   AlphaFoldDB; P28475; -.
DR   SMR; P28475; -.
DR   STRING; 3750.XP_008382366.1; -.
DR   EnsemblPlants; mRNA:MD10G0051500; mRNA:MD10G0051500; MD10G0051500.
DR   GeneID; 103445158; -.
DR   Gramene; mRNA:MD10G0051500; mRNA:MD10G0051500; MD10G0051500.
DR   KEGG; mdm:103445158; -.
DR   OrthoDB; 1016440at2759; -.
DR   BioCyc; MetaCyc:MON-11700; -.
DR   BRENDA; 1.1.1.200; 3164.
DR   GO; GO:0047641; F:aldose-6-phosphate reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   CDD; cd19112; AKR_AKR2A1-2; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044485; AKR2A1.
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   NADP; Oxidoreductase.
FT   CHAIN           1..310
FT                   /note="NADP-dependent D-sorbitol-6-phosphate dehydrogenase"
FT                   /id="PRO_0000124657"
FT   ACT_SITE        48
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..272
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            77
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  34905 MW;  DECCAD94BF5E6D9F CRC64;
     MSTVTLSSGY EMPVIGLGLW RLEKDELKEV ILNAIKIGYR HFDCAAHYKS EADVGEALAE
     AFKTGLVKRE ELFITTKIWN SDHGHVVEAC KNSLEKLQID YLDLYLVHYP MPTKHNAIGK
     TASLLGEDKV LDIDVTISLQ QTWEGMEKTV SLGLVRSIGL SNYELFLTRD CLAYSKIKPA
     VSQFETHPYF QRDSLVKFCM KHGVLPTAHT PLGGAAANKD MFGSVSPLDD PVLNDVAKKY
     GKSVAQICLR WGIQRKTAVI PKSSKIQRLK ENLEVLEFQL SDEDMQLIYS IDRKYRTSLP
     SKTWGLDVYA