ID DPEP_SOLTU Reviewed; 576 AA. AC Q06801; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=4-alpha-glucanotransferase, chloroplastic/amyloplastic; DE EC=2.4.1.25; DE AltName: Full=Amylomaltase; DE AltName: Full=Disproportionating enzyme; DE Short=D-enzyme; DE Flags: Precursor; GN Name=DPEP; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 53-57; 174-183 AND RP 247-259. RC STRAIN=cv. May Queen; TISSUE=Tuber; RX PubMed=7678257; DOI=10.1016/s0021-9258(18)54088-6; RA Takaha T., Yanase M., Okada S., Smith S.M.; RT "Disproportionating enzyme (4-alpha-glucanotransferase; EC 2.4.1.25) of RT potato. Purification, molecular cloning, and potential role in starch RT metabolism."; RL J. Biol. Chem. 268:1391-1396(1993). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 53-576. RA Imamura K., Matsuura T., Takaha T., Fujii K., Nakagawa A., Kusunoki M., RA Nitta Y.; RT "Structure determination and refinement at 1.8 A resolution of RT disproportionating enzyme from potato."; RL Submitted (APR-2005) to the PDB data bank. CC -!- FUNCTION: May act during starch breakdown to convert small CC oligosaccharides into larger molecules upon which starch phosphorylase CC can act, or may change the structure of starch molecules and grain CC architecture by modifying chain length, or may generate from starch and CC glucose oligosaccharides which can serve either as primers for new CC starch phosphoenzyme. 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 -!- TISSUE SPECIFICITY: Present in leaves, stems, roots, and stolons but is CC most abundant in developing and mature tubers. 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; X68664; CAA48630.1; -; mRNA. DR PIR; A45049; A45049. DR RefSeq; NP_001274781.1; NM_001287852.1. DR PDB; 1X1N; X-ray; 1.80 A; A=53-576. DR PDB; 6LX1; X-ray; 2.03 A; A=53-576. DR PDB; 6LX2; X-ray; 2.05 A; A=53-576. DR PDB; 7COV; X-ray; 2.00 A; A=1-576. DR PDBsum; 1X1N; -. DR PDBsum; 6LX1; -. DR PDBsum; 6LX2; -. DR PDBsum; 7COV; -. DR AlphaFoldDB; Q06801; -. DR SMR; Q06801; -. DR STRING; 4113.Q06801; -. DR CAZy; GH77; Glycoside Hydrolase Family 77. DR PaxDb; 4113-PGSC0003DMT400042739; -. DR GeneID; 102595076; -. DR KEGG; sot:102595076; -. DR eggNOG; ENOG502QU40; Eukaryota. DR InParanoid; Q06801; -. DR OrthoDB; 201724at2759; -. DR BRENDA; 2.4.1.25; 5757. DR EvolutionaryTrace; Q06801; -. DR Proteomes; UP000011115; Unassembled WGS sequence. DR ExpressionAtlas; Q06801; differential. DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. 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 Direct protein sequencing; Glycosyltransferase; Plastid; KW Reference proteome; Transferase; Transit peptide. FT TRANSIT 1..52 FT /note="Chloroplast" FT /evidence="ECO:0000269|PubMed:7678257" FT CHAIN 53..576 FT /note="4-alpha-glucanotransferase, FT chloroplastic/amyloplastic" FT /id="PRO_0000018550" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 79..83 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:6LX2" FT HELIX 100..112 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 151..156 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:1X1N" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 179..196 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 200..210 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 212..231 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 236..238 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 241..244 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 248..257 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 259..285 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 289..297 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 303..306 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 320..326 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 329..333 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 336..341 FT /evidence="ECO:0007829|PDB:6LX1" FT HELIX 345..350 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 354..366 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 368..373 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 375..378 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 380..385 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 389..393 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 395..398 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 402..412 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 416..419 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 427..435 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 440..443 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 444..446 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 447..450 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 458..460 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 463..469 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 477..482 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 486..495 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 501..503 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 504..513 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 518..523 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 524..527 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 532..534 FT /evidence="ECO:0007829|PDB:1X1N" FT STRAND 542..544 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 556..558 FT /evidence="ECO:0007829|PDB:1X1N" FT HELIX 560..572 FT /evidence="ECO:0007829|PDB:1X1N" SQ SEQUENCE 576 AA; 64951 MW; A0D16F3A546307BB CRC64; MAIHTCFSLI PSSFSSPKLP YPKNTTFQSP IPKLSRPTFM FDRKGSFQNG TAAVPAVGED FPIDYADWLP KRDPNDRRRA GILLHPTSFP GPYGIGDLGP QAFKFLDWLH LAGCSLWQVL PLVPPGKRGN EDGSPYSGQD ANCGNTLLIS LEELVDDGLL KMEELPEPLP TDRVNYSTIS EIKDPLITKA AKRLLSSEGE LKDQLENFRR DPNISSWLED AAYFAAIDNS VNTISWYDWP EPLKNRHLAA LEEVYQSEKD FIDIFIAQQF LFQRQWKKVR DYARSKGISI MGDMPIYVGY HSADVWANKK QFLLNRKGFP LIVSGVPPDA FSETGQLWGS PLYDWKAMEK DGFSWWVRRI QRATDLFDEF RIDHFRGFAG FWAVPSEEKI AILGRWKVGP GKPLFDAILQ AVGKINIIAE DLGVITEDVV QLRKSIEAPG MAVLQFAFGS DAENPHLPHN HEQNQVVYTG THDNDTIRGW WDTLPQEEKS NVLKYLSNIE EEEISRGLIE GAVSSVARIA IIPMQDVLGL GSDSRMNIPA TQFGNWSWRI PSSTSFDNLD AEAKKLRDIL ATYGRL //