ID   DPE2_ARATH              Reviewed;         955 AA.
AC   Q8RXD9; O22198;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=4-alpha-glucanotransferase DPE2;
DE            EC=2.4.1.25;
DE   AltName: Full=Amylomaltase;
DE   AltName: Full=Disproportionating enzyme;
DE            Short=D-enzyme;
DE   AltName: Full=Protein DISPROPORTIONATING ENZYME 2;
GN   Name=DPE2; OrderedLocusNames=At2g40840; ORFNames=T20B5.4;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   DISRUPTION PHENOTYPE, AND INDUCTION.
RX   PubMed=14593480; DOI=10.1007/s00425-003-1127-z;
RA   Lu Y., Sharkey T.D.;
RT   "The role of amylomaltase in maltose metabolism in the cytosol of
RT   photosynthetic cells.";
RL   Planta 218:466-473(2004).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=14996213; DOI=10.1111/j.1365-313x.2003.02012.x;
RA   Chia T., Thorneycroft D., Chapple A., Messerli G., Chen J., Zeeman S.C.,
RA   Smith S.M., Smith A.M.;
RT   "A cytosolic glucosyltransferase is required for conversion of starch to
RT   sucrose in Arabidopsis leaves at night.";
RL   Plant J. 37:853-863(2004).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15665241; DOI=10.1104/pp.104.055996;
RA   Weise S.E., Kim K.S., Stewart R.P., Sharkey T.D.;
RT   "beta-Maltose is the metabolically active anomer of maltose during
RT   transitory starch degradation.";
RL   Plant Physiol. 137:756-761(2005).
RN   [7]
RP   INDUCTION.
RX   PubMed=16055686; DOI=10.1104/pp.105.061903;
RA   Lu Y., Gehan J.P., Sharkey T.D.;
RT   "Daylength and circadian effects on starch degradation and maltose
RT   metabolism.";
RL   Plant Physiol. 138:2280-2291(2005).
RN   [8]
RP   FUNCTION.
RX   PubMed=17028209; DOI=10.1105/tpc.105.037671;
RA   Dumez S., Wattebled F., Dauvillee D., Delvalle D., Planchot V., Ball S.G.,
RA   D'Hulst C.;
RT   "Mutants of Arabidopsis lacking starch branching enzyme II substitute
RT   plastidial starch synthesis by cytoplasmic maltose accumulation.";
RL   Plant Cell 18:2694-2709(2006).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16596410; DOI=10.1007/s00425-006-0263-7;
RA   Lu Y., Steichen J.M., Weise S.E., Sharkey T.D.;
RT   "Cellular and organ level localization of maltose in maltose-excess
RT   Arabidopsis mutants.";
RL   Planta 224:935-943(2006).
RN   [10]
RP   FUNCTION.
RX   PubMed=16640603; DOI=10.1111/j.1365-313x.2006.02732.x;
RA   Fettke J., Chia T., Eckermann N., Smith A., Steup M.;
RT   "A transglucosidase necessary for starch degradation and maltose metabolism
RT   in leaves at night acts on cytosolic heteroglycans (SHG).";
RL   Plant J. 46:668-684(2006).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
RN   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20700743; DOI=10.1007/s00425-010-1245-3;
RA   Luetken H., Lloyd J.R., Glaring M.A., Baunsgaard L., Laursen K.H.,
RA   Haldrup A., Kossmann J., Blennow A.;
RT   "Repression of both isoforms of disproportionating enzyme leads to higher
RT   malto-oligosaccharide content and reduced growth in potato.";
RL   Planta 232:1127-1139(2010).
RN   [13]
RP   FUNCTION.
RX   PubMed=21269731; DOI=10.1016/j.jplph.2010.12.008;
RA   Malinova I., Steup M., Fettke J.;
RT   "Starch-related cytosolic heteroglycans in roots from Arabidopsis
RT   thaliana.";
RL   J. Plant Physiol. 168:1406-1414(2011).
RN   [14]
RP   FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21242321; DOI=10.1093/mp/ssq078;
RA   Li T., Xu S.L., Oses-Prieto J.A., Putil S., Xu P., Wang R.J., Li K.H.,
RA   Maltby D.A., An L.H., Burlingame A.L., Deng Z.P., Wang Z.Y.;
RT   "Proteomics analysis reveals post-translational mechanisms for cold-induced
RT   metabolic changes in Arabidopsis.";
RL   Mol. Plant 4:361-374(2011).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Cytosolic alpha-glucanotransferase essential for the
CC       cytosolic metabolism of maltose, an intermediate on the pathway by
CC       which starch is converted to sucrose in leaves at night. Metabolizes
CC       maltose exported from the chloroplast and is specific for beta-maltose.
CC       May play a role in freezing tolerance. Temperature drop induces
CC       inactivation of DPE2 that leads to rapid accumulation of maltose, a
CC       solute that protects cells from freezing damage.
CC       {ECO:0000269|PubMed:14996213, ECO:0000269|PubMed:16640603,
CC       ECO:0000269|PubMed:17028209, ECO:0000269|PubMed:21242321,
CC       ECO:0000269|PubMed:21269731}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC         position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC         glucan.; EC=2.4.1.25;
CC   -!- ACTIVITY REGULATION: Inactivated in response to cold stress.
CC       {ECO:0000269|PubMed:21242321}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14996213,
CC       ECO:0000269|PubMed:16596410, ECO:0000269|PubMed:20700743}.
CC   -!- INDUCTION: Circadian-regulation with a peak in expression in the middle
CC       of the light period. {ECO:0000269|PubMed:14593480,
CC       ECO:0000269|PubMed:16055686}.
CC   -!- DISRUPTION PHENOTYPE: Dwarf plants with yellowish leaves that
CC       accumulate large amounts of maltose. Increased tolerance to cold.
CC       {ECO:0000269|PubMed:14593480, ECO:0000269|PubMed:14996213,
CC       ECO:0000269|PubMed:15665241, ECO:0000269|PubMed:21242321}.
CC   -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB86444.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC002409; AAB86444.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC09889.1; -; Genomic_DNA.
DR   EMBL; AY081315; AAL91204.1; -; mRNA.
DR   EMBL; BT010364; AAQ56807.1; -; mRNA.
DR   PIR; T00748; T00748.
DR   RefSeq; NP_181616.3; NM_129647.4.
DR   AlphaFoldDB; Q8RXD9; -.
DR   SMR; Q8RXD9; -.
DR   BioGRID; 4019; 3.
DR   STRING; 3702.Q8RXD9; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   iPTMnet; Q8RXD9; -.
DR   PaxDb; 3702-AT2G40840-1; -.
DR   ProteomicsDB; 220485; -.
DR   EnsemblPlants; AT2G40840.1; AT2G40840.1; AT2G40840.
DR   GeneID; 818682; -.
DR   Gramene; AT2G40840.1; AT2G40840.1; AT2G40840.
DR   KEGG; ath:AT2G40840; -.
DR   Araport; AT2G40840; -.
DR   TAIR; AT2G40840; DPE2.
DR   eggNOG; ENOG502QR3V; Eukaryota.
DR   HOGENOM; CLU_014132_0_0_1; -.
DR   InParanoid; Q8RXD9; -.
DR   OMA; WTDSYPY; -.
DR   OrthoDB; 4592at2759; -.
DR   PhylomeDB; Q8RXD9; -.
DR   BioCyc; ARA:AT2G40840-MONOMER; -.
DR   BRENDA; 2.4.1.25; 399.
DR   PRO; PR:Q8RXD9; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8RXD9; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IDA:TAIR.
DR   GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010297; F:heteropolysaccharide binding; IDA:TAIR.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0000025; P:maltose catabolic process; IDA:TAIR.
DR   GO; GO:0000023; P:maltose metabolic process; IMP:TAIR.
DR   GO; GO:0005976; P:polysaccharide metabolic process; TAS:TAIR.
DR   GO; GO:0005983; P:starch catabolic process; TAS:TAIR.
DR   CDD; cd05815; CBM20_DPE2_repeat1; 1.
DR   CDD; cd05816; CBM20_DPE2_repeat2; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR034840; CBM20_DPE2_1.
DR   InterPro; IPR034841; CBM20_DPE2_2.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR003385; Glyco_hydro_77.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR32518; -; 1.
DR   PANTHER; PTHR32518:SF3; 4-ALPHA-GLUCANOTRANSFERASE; 1.
DR   Pfam; PF00686; CBM_20; 2.
DR   Pfam; PF02446; Glyco_hydro_77; 1.
DR   SMART; SM01065; CBM_2; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 2.
DR   PROSITE; PS51166; CBM20; 2.
DR   Genevisible; Q8RXD9; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Carbohydrate metabolism; Cytoplasm; Glycosyltransferase;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..955
FT                   /note="4-alpha-glucanotransferase DPE2"
FT                   /id="PRO_0000407919"
FT   DOMAIN          13..122
FT                   /note="CBM20 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT   DOMAIN          157..270
FT                   /note="CBM20 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT   REGION          925..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   955 AA;  109777 MW;  248BCED6B0CE79BC CRC64;
     MMNLGSLSLS TSKSSKPMVS ISFWIPYFTH WGESLLVCGS APGLGSGNVK KGLLLKPSQQ
     DDQLIWSGSV SVPPGFSSDY CYYVVDDSKS VLRSEFGMKR KLVVPETLTG GESVHLRDLW
     QSGDQALPFR SAFKDVIFHH SFDVKVEKPL GVFMNKSDQD DSVVVQFKIC CPDIGEGTSV
     YVLGTPEKLG NWKVENGLRL NYVDDSIWEA DCLIPKADFP IKYRYCKVQK EDSIGFESGG
     NRELSLHSIG SKQEYIVMSD GLFRAMPWRG AGVAVPMFSV RSEDDVGVGE FLDLKLLVDW
     AVDSGLHLVQ LLPVNDTSVH KMWWDSYPYS SLSVFALHPL YLRVQALSER LPEDIKEEIQ
     KAKNQLDKND VDYEATMETK LSIAKKIFDI EKDQTLNSST FQKFFSENEG WLKPYAAFCF
     LRDFFETSDH SQWGTFSDYT DDKLEKLISK DNLHYNTICF HYYIQYHLHV QLSAAAEYAR
     KKGVVLKGDL PIGVDRNSVD TWVYRNLFRM NTSTGAPPDY FDKNGQNWGF PTYNWEEMSK
     DNYAWWRARL TQMGKYFTAY RIDHILGFFR IWELPAHAMT GLVGKFRPSI PLSQEELEKE
     GIWDFDRLSK PYIQKKFLEE KFGDFWPFIA SNFLNETQKD MYEFKEDCNT EKKIVAKLKS
     LAEKSLLLEN EDKVRRDVFD ILRNVVLIKD PEDARKFYPR FNIEDTSSFQ DLDDHSKNVL
     KRLYYDYYFQ RQEDLWRKNA LKTLPALLNS SNMLACGEDL GLIPSCVHPV MQELGLVGLR
     IQRMPSESDV KFGIPSNYDY MTVCAPSCHD CSTLRAWWEE DEERRQQYFK EVIGVDGIPP
     SQCIPEITHF ILRQHVEAPS MWAIFPLQDM MALKEEYTTR PATEETINDP TNPKHYWRYR
     VHVTLDSLLK DTDLKSTIKN LVSSSGRSVP ANVSGEDINK SRGEVIANGS TKPNP
//