MALQ_THETH
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 03-AUG-2022, entry version 102.
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; Deinococcus-Thermus; 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}.
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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 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; 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
