DPEP_SOLTU
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 03-AUG-2022, entry version 108.
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}.
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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.PGSC0003DMT400042739; -.
DR CAZy; GH77; Glycoside Hydrolase Family 77.
DR PRIDE; Q06801; -.
DR GeneID; 102595076; -.
DR KEGG; sot:102595076; -.
DR eggNOG; ENOG502QU40; Eukaryota.
DR InParanoid; Q06801; -.
DR OrthoDB; 302364at2759; -.
DR BRENDA; 2.4.1.25; 5757.
DR EvolutionaryTrace; Q06801; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q06801; baseline.
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 InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR32438; PTHR32438; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR TIGRFAMs; TIGR00217; malQ; 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
