DHSO_ARATH
ID DHSO_ARATH Reviewed; 364 AA.
AC Q9FJ95; B9DHK6; Q67XB8; Q8LEV5;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Sorbitol dehydrogenase {ECO:0000303|PubMed:23498864};
DE Short=SDH {ECO:0000303|PubMed:23498864};
DE EC=1.1.1.- {ECO:0000269|PubMed:23498864};
DE AltName: Full=Polyol dehydrogenase {ECO:0000305|PubMed:23498864};
DE AltName: Full=Ribitol dehydrogenase {ECO:0000303|PubMed:23498864};
DE Short=RDH {ECO:0000303|PubMed:23498864};
DE EC=1.1.1.56 {ECO:0000269|PubMed:23498864};
DE AltName: Full=Xylitol dehydrogenase {ECO:0000303|PubMed:23498864};
DE Short=XDH {ECO:0000303|PubMed:23498864};
DE EC=1.1.1.9 {ECO:0000269|PubMed:23498864};
GN Name=SDH; OrderedLocusNames=At5g51970; ORFNames=MSG15.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-364.
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=23498864; DOI=10.1016/j.plantsci.2013.01.012;
RA Aguayo M.F., Ampuero D., Mandujano P., Parada R., Munoz R., Gallart M.,
RA Altabella T., Cabrera R., Stange C., Handford M.;
RT "Sorbitol dehydrogenase is a cytosolic protein required for sorbitol
RT metabolism in Arabidopsis thaliana.";
RL Plant Sci. 206:63-75(2013).
CC -!- FUNCTION: Polyol dehydrogenase that catalyzes the NAD(+)-dependent
CC oxidation of various sugar alcohols. Is mostly active with D-sorbitol
CC (D-glucitol), ribitol and xylitol as substrates, leading to the C2-
CC oxidized products D-fructose, D-ribulose and D-xylulose, respectively.
CC To a lesser extent, can also oxidize arabitol, mannitol, lactitol and
CC maltitol in vitro. Is required for sorbitol metabolism. Cannot use
CC NADP(+) as the electron acceptor. {ECO:0000269|PubMed:23498864}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + keto-D-fructose + NADH = D-sorbitol + NAD(+);
CC Xref=Rhea:RHEA:33031, ChEBI:CHEBI:15378, ChEBI:CHEBI:17924,
CC ChEBI:CHEBI:48095, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:23498864};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33033;
CC Evidence={ECO:0000269|PubMed:23498864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + ribitol = D-ribulose + H(+) + NADH;
CC Xref=Rhea:RHEA:20053, ChEBI:CHEBI:15378, ChEBI:CHEBI:15963,
CC ChEBI:CHEBI:17173, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.56;
CC Evidence={ECO:0000269|PubMed:23498864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + xylitol = D-xylulose + H(+) + NADH;
CC Xref=Rhea:RHEA:20433, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC ChEBI:CHEBI:17151, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.9;
CC Evidence={ECO:0000269|PubMed:23498864};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for sorbitol {ECO:0000269|PubMed:23498864};
CC KM=0.07 mM for NAD(+) {ECO:0000269|PubMed:23498864};
CC Note=kcat is 0.33 sec(-1) towards sorbitol for the reaction with
CC sorbitol as substrate. kcat is 0.39 sec(-1) towards NAD(+) for the
CC reaction with sorbitol as substrate. {ECO:0000269|PubMed:23498864};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Cell membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:23498864}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in dry seeds and leaves, and, to a
CC lower extent, in roots, stems, flowers and siliques (at protein level).
CC {ECO:0000269|PubMed:23498864}.
CC -!- DISRUPTION PHENOTYPE: Reduced dry weight and primary root length when
CC grown in the presence of sorbitol. Increased resistance to dehydration
CC under short-day conditions. {ECO:0000269|PubMed:23498864}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AB015478; BAB11045.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96152.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96153.1; -; Genomic_DNA.
DR EMBL; AF370161; AAK43976.1; -; mRNA.
DR EMBL; AY133848; AAM91782.1; -; mRNA.
DR EMBL; AK176901; BAD44664.1; -; mRNA.
DR EMBL; AK230367; BAF02166.1; -; mRNA.
DR EMBL; AY085213; AAM62446.1; -; mRNA.
DR EMBL; AK317559; BAH20223.1; -; mRNA.
DR RefSeq; NP_200010.1; NM_124576.3.
DR RefSeq; NP_974925.1; NM_203196.1.
DR AlphaFoldDB; Q9FJ95; -.
DR SMR; Q9FJ95; -.
DR BioGRID; 20517; 1.
DR STRING; 3702.AT5G51970.1; -.
DR PaxDb; Q9FJ95; -.
DR PRIDE; Q9FJ95; -.
DR ProteomicsDB; 224244; -.
DR EnsemblPlants; AT5G51970.1; AT5G51970.1; AT5G51970.
DR EnsemblPlants; AT5G51970.2; AT5G51970.2; AT5G51970.
DR GeneID; 835272; -.
DR Gramene; AT5G51970.1; AT5G51970.1; AT5G51970.
DR Gramene; AT5G51970.2; AT5G51970.2; AT5G51970.
DR KEGG; ath:AT5G51970; -.
DR Araport; AT5G51970; -.
DR TAIR; locus:2173093; AT5G51970.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_5_1; -.
DR InParanoid; Q9FJ95; -.
DR OMA; ETWYAMS; -.
DR OrthoDB; 1019156at2759; -.
DR PhylomeDB; Q9FJ95; -.
DR BioCyc; ARA:AT5G51970-MON; -.
DR PRO; PR:Q9FJ95; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ95; baseline and differential.
DR Genevisible; Q9FJ95; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0046526; F:D-xylulose reductase activity; IDA:TAIR.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0050255; F:ribitol 2-dehydrogenase activity; IDA:TAIR.
DR GO; GO:0009010; F:sorbitol-6-phosphate 2-dehydrogenase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006060; P:sorbitol metabolic process; IDA:TAIR.
DR CDD; cd05285; sorbitol_DH; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR045306; SDH-like.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Metal-binding; Mitochondrion; NAD;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..364
FT /note="Sorbitol dehydrogenase"
FT /id="PRO_0000422084"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 284..286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 308..310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT CONFLICT 65
FT /note="R -> I (in Ref. 4; BAD44664)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="R -> Q (in Ref. 5; AAM62446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 39256 MW; 8FCF9ED97352FD48 CRC64;
MGKGGMSQGE GSKVEEENMA AWLVGINTLK IQPFLLPSVG PHDVRVRMKA VGICGSDVHY
LKTMRCADFV VKEPMVIGHE CAGIIEEVGE EVKHLVVGDR VALEPGISCW RCNLCREGRY
NLCPEMKFFA TPPVHGSLAN QVVHPADLCF KLPENVSLEE GAMCEPLSVG VHACRRAEVG
PETNVLVMGA GPIGLVTMLA ARAFSVPRIV IVDVDENRLA VAKQLGADEI VQVTTNLEDV
GSEVEQIQKA MGSNIDVTFD CAGFNKTMST ALAATRCGGK VCLVGMGHGI MTVPLTPAAA
REVDVVGVFR YKNTWPLCLE FLTSGKIDVK PLITHRFGFS QKEVEDAFET SARGSNAIKV
MFNL
