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}.
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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 Genevisible; Q9LV91; AT.
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.
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
//
