ID DPE1_ARATH Reviewed; 576 AA. AC Q9LV91; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 131. DE RecName: Full=4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic; 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 1; DE Flags: Precursor; GN Name=DPE1; OrderedLocusNames=At5g64860; ORFNames=MXK3.9; 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=10718197; DOI=10.1093/dnares/7.1.31; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:31-63(2000). 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 FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=11359613; DOI=10.1046/j.1365-313x.2001.01012.x; RA Critchley J.H., Zeeman S.C., Takaha T., Smith A.M., Smith S.M.; RT "A critical role for disproportionating enzyme in starch breakdown is RT revealed by a knock-out mutation in Arabidopsis."; RL Plant J. 26:89-100(2001). RN [5] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=19946617; DOI=10.1093/mp/ssp093; RA Stettler M., Eicke S., Mettler T., Messerli G., Hoertensteiner S., RA Zeeman S.C.; RT "Blocking the metabolism of starch breakdown products in Arabidopsis leaves RT triggers chloroplast degradation."; RL Mol. Plant 2:1233-1246(2009). CC -!- FUNCTION: Chloroplastic alpha-glucanotransferase involved in CC maltotriose metabolism. Probably uses maltotriose as substrate to CC transfer a maltosyl unit from one molecule to another, resulting in CC glucose and maltopentaose. The latter can then be further metabolized CC to maltose and maltotriose by beta-amylase. Required for normal starch CC degradation in leaves. {ECO:0000269|PubMed:11359613, CC ECO:0000269|PubMed:19946617}. 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast CC {ECO:0000305}. CC -!- DISRUPTION PHENOTYPE: Increased amounts of maltotriose and leaf starch. CC {ECO:0000269|PubMed:11359613, ECO:0000269|PubMed:19946617}. CC -!- SIMILARITY: Belongs to the disproportionating enzyme family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB019236; BAA97298.1; -; Genomic_DNA. DR EMBL; CP002688; AED97962.1; -; Genomic_DNA. DR EMBL; AY037231; AAK59831.1; -; mRNA. DR EMBL; AY081744; AAL87397.1; -; mRNA. DR RefSeq; NP_201291.1; NM_125884.4. DR PDB; 5CPQ; X-ray; 2.13 A; A/B=46-576. DR PDB; 5CPS; X-ray; 1.80 A; A/B=46-576. DR PDB; 5CPT; X-ray; 2.30 A; A/B=46-576. DR PDB; 5CQ1; X-ray; 2.30 A; A/B=46-576. DR PDB; 5CSU; X-ray; 2.53 A; A/B=46-576. DR PDB; 5CSY; X-ray; 2.05 A; A/B=46-576. DR PDBsum; 5CPQ; -. DR PDBsum; 5CPS; -. DR PDBsum; 5CPT; -. DR PDBsum; 5CQ1; -. DR PDBsum; 5CSU; -. DR PDBsum; 5CSY; -. DR AlphaFoldDB; Q9LV91; -. DR SMR; Q9LV91; -. DR STRING; 3702.Q9LV91; -. DR CAZy; GH77; Glycoside Hydrolase Family 77. DR iPTMnet; Q9LV91; -. DR PaxDb; 3702-AT5G64860-1; -. DR ProteomicsDB; 241246; -. DR EnsemblPlants; AT5G64860.1; AT5G64860.1; AT5G64860. DR GeneID; 836609; -. DR Gramene; AT5G64860.1; AT5G64860.1; AT5G64860. DR KEGG; ath:AT5G64860; -. DR Araport; AT5G64860; -. DR TAIR; AT5G64860; DPE1. DR eggNOG; ENOG502QU40; Eukaryota. DR HOGENOM; CLU_014132_1_0_1; -. DR InParanoid; Q9LV91; -. DR OMA; TGQLWGT; -. DR OrthoDB; 201724at2759; -. DR PhylomeDB; Q9LV91; -. DR BioCyc; ARA:AT5G64860-MONOMER; -. DR BioCyc; MetaCyc:AT5G64860-MONOMER; -. DR BRENDA; 2.4.1.25; 399. DR PRO; PR:Q9LV91; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q9LV91; baseline and differential. DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell. DR GO; GO:0009507; C:chloroplast; HDA:TAIR. DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IMP:UniProtKB. DR GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006006; P:glucose metabolic process; IMP:TAIR. DR GO; GO:0000025; P:maltose catabolic process; IMP:UniProtKB. DR GO; GO:0005983; P:starch catabolic process; IMP:UniProtKB. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR003385; Glyco_hydro_77. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR NCBIfam; TIGR00217; malQ; 1. DR PANTHER; PTHR32438; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC/AMYLOPLASTIC; 1. DR PANTHER; PTHR32438:SF5; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC_AMYLOPLASTIC; 1. DR Pfam; PF02446; Glyco_hydro_77; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR Genevisible; Q9LV91; AT. PE 1: Evidence at protein level; KW 3D-structure; Amyloplast; Carbohydrate metabolism; Chloroplast; KW Glycosyltransferase; Plastid; Reference proteome; Transferase; KW Transit peptide. FT TRANSIT 1..45 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 46..576 FT /note="4-alpha-glucanotransferase DPE1, FT chloroplastic/amyloplastic" FT /id="PRO_0000407918" FT HELIX 69..71 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 96..99 FT /evidence="ECO:0007829|PDB:5CPQ" FT HELIX 104..116 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:5CSU" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 151..156 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 176..196 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 200..210 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 212..230 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 236..238 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 241..244 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 248..257 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 259..285 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 289..297 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 303..306 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 307..311 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 320..326 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 332..334 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 336..341 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 345..349 FT /evidence="ECO:0007829|PDB:5CPS" FT TURN 350..353 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 354..366 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 368..373 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 375..378 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 380..385 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 395..398 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 402..412 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 417..419 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 427..436 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 440..443 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 444..446 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 449..451 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 458..460 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 463..469 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 477..483 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 486..495 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 501..503 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 504..514 FT /evidence="ECO:0007829|PDB:5CPS" FT STRAND 518..523 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 524..527 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 532..534 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 556..558 FT /evidence="ECO:0007829|PDB:5CPS" FT HELIX 560..572 FT /evidence="ECO:0007829|PDB:5CPS" SQ SEQUENCE 576 AA; 64412 MW; 1363A43AF365A491 CRC64; MSILLRPSSS PSLCSSLKLF RLSSPDSLID AAVLRNRTKP SQSFRMEVVS SNSTCLSSIS VGEDFPSEYE QWLPVPDPES RRRAGVLLHP TSFRGPHGIG DLGEEAFRFI DWLHSTGCSV WQVLPLVPPD EGGSPYAGQD ANCGNTLLIS LDELVKDGLL IKDELPQPID ADSVNYQTAN KLKSPLITKA AKRLIDGNGE LKSKLLDFRN DPSISCWLED AAYFAAIDNT LNAYSWFEWP EPLKNRHLSA LEAIYESQKE FIDLFIAKQF LFQRQWQKVR EYARRQGVDI MGDMPIYVGY HSADVWANKK HFLLNKKGFP LLVSGVPPDL FSETGQLWGS PLYDWKAMES DQYSWWVNRI RRAQDLYDEC RIDHFRGFAG FWAVPSEAKV AMVGRWKVGP GKSLFDAISK GVGKIKIIAE DLGVITKDVV ELRKSIGAPG MAVLQFAFGG GADNPHLPHN HEVNQVVYSG THDNDTIRGW WDTLDQEEKS KAMKYLSIAG EDDISWSVIQ AAFSSTAQTA IIPMQDILGL GSSARMNTPA TEVGNWGWRI PSSTSFDNLE TESDRLRDLL SLYGRL //