ID MALQ_THETH Reviewed; 500 AA. AC O87172; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 107. DE RecName: Full=4-alpha-glucanotransferase; DE EC=2.4.1.25; DE AltName: Full=Amylomaltase; DE AltName: Full=Disproportionating enzyme; DE Short=D-enzyme; GN Name=malQ; OS Thermus thermophilus. OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33923 / DSM 674 / AT-62; RA Terada Y., Fujii K., Takaha T., Okada S.; RT "Cloning, expression and characterization of amylomaltase from Thermus RT aquaticus ATCC33923."; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=10677288; DOI=10.1006/jmbi.1999.3503; RA Przylas I., Tomoo K., Terada Y., Takaha T., Fujii K., Saenger W., RA Strater N.; RT "Crystal structure of amylomaltase from Thermus aquaticus, a RT glycosyltransferase catalysing the production of large cyclic glucans."; RL J. Mol. Biol. 296:873-886(2000). 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: Cytoplasm {ECO:0000250}. 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; AB016244; BAA33728.1; -; Genomic_DNA. DR PDB; 1CWY; X-ray; 2.00 A; A=1-500. DR PDB; 1ESW; X-ray; 1.90 A; A=1-500. DR PDB; 1FP8; X-ray; 2.30 A; A=1-500. DR PDB; 1FP9; X-ray; 3.10 A; A=1-500. DR PDB; 2OWC; X-ray; 2.05 A; A=1-500. DR PDB; 2OWW; X-ray; 2.20 A; A=1-500. DR PDB; 2OWX; X-ray; 2.50 A; A=1-500. DR PDB; 5JIW; X-ray; 1.73 A; A=1-500. DR PDBsum; 1CWY; -. DR PDBsum; 1ESW; -. DR PDBsum; 1FP8; -. DR PDBsum; 1FP9; -. DR PDBsum; 2OWC; -. DR PDBsum; 2OWW; -. DR PDBsum; 2OWX; -. DR PDBsum; 5JIW; -. DR AlphaFoldDB; O87172; -. DR SMR; O87172; -. DR CAZy; GH77; Glycoside Hydrolase Family 77. DR BRENDA; 2.4.1.25; 2305. DR EvolutionaryTrace; O87172; -. DR GO; GO:0005737; C:cytoplasm; 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; Carbohydrate metabolism; Cytoplasm; Glycosyltransferase; KW Transferase. FT CHAIN 1..500 FT /note="4-alpha-glucanotransferase" FT /id="PRO_0000170132" FT STRAND 5..10 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 13..15 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 19..22 FT /evidence="ECO:0007829|PDB:1ESW" FT HELIX 27..38 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 69..71 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 75..79 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 97..118 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 121..133 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 135..150 FT /evidence="ECO:0007829|PDB:5JIW" FT TURN 151..153 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 161..164 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 168..177 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 179..205 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 209..217 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 223..227 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 240..246 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 256..261 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 265..270 FT /evidence="ECO:0007829|PDB:5JIW" FT TURN 271..273 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 274..286 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 288..293 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 295..298 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 300..305 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 315..318 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 321..332 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 347..355 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 360..363 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 364..366 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 367..370 FT /evidence="ECO:0007829|PDB:1ESW" FT HELIX 378..380 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 387..391 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 399..405 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 408..420 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 428..430 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 431..441 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 445..450 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 451..454 FT /evidence="ECO:0007829|PDB:5JIW" FT HELIX 459..461 FT /evidence="ECO:0007829|PDB:5JIW" FT STRAND 469..471 FT /evidence="ECO:0007829|PDB:1ESW" FT TURN 479..481 FT /evidence="ECO:0007829|PDB:2OWW" FT HELIX 484..496 FT /evidence="ECO:0007829|PDB:5JIW" SQ SEQUENCE 500 AA; 57222 MW; 6E7175A38E0A5D61 CRC64; MELPRAFGLL LHPTSLPGPY GVGVLGREAR DFLRFLKEAG GRYWQVLPLG PTGYGDSPYQ SFSAFAGNPY LIDLRPLAER GYVRLEDPGF PQGRVDYGLL YAWKWPALKE AFRGFKEKAS PEEREAFAAF REREAWWLED YALFMALKGA HGGLPWNRWP LPLRKREEKA LREAKSALAE EVAFHAFTQW LFFRQWGALK AEAEALGIRI IGDMPIFVAE DSAEVWAHPE WFHLDEEGRP TVVAGVPPDY FSETGQRWGN PLYRWDVLER EGFSFWIRRL EKALELFHLV RIDHFRGFEA YWEIPASCPT AVEGRWVKAP GEKLFQKIQE VFGEVPVLAE DLGVITPEVE ALRDRFGLPG MKVLQFAFDD GMENPFLPHN YPAHGRVVVY TGTHDNDTTL GWYRTATPHE KAFMARYLAD WGITFREEEE VPWALMHLGM KSVARLAVYP VQDVLALGSE ARMNYPGRPS GNWAWRLLPG ELSPEHGARL RAMAEATERL //