BE_THET8
ID BE_THET8 Reviewed; 520 AA.
AC Q5SH28; P84162;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=1,4-alpha-glucan branching enzyme TTHA1902;
DE EC=2.4.1.18;
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase;
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme;
DE AltName: Full=Branching enzyme;
DE Short=BE;
GN OrderedLocusNames=TTHA1902; ORFNames=TT1467;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of TT1467 from Thermus thermophilus HB8.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP MUTAGENESIS OF PHE-23; GLU-184; TYR-236; LEU-271; TRP-274; ASP-353;
RP TRP-360; TRP-404 AND PHE-463.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=21097495; DOI=10.1074/jbc.m110.179515;
RA Palomo M., Pijning T., Booiman T., Dobruchowska J.M., van der Vlist J.,
RA Kralj S., Planas A., Loos K., Kamerling J.P., Dijkstra B.W.,
RA van der Maarel M.J., Dijkhuizen L., Leemhuis H.;
RT "Thermus thermophilus glycoside hydrolase family 57 branching enzyme:
RT crystal structure, mechanism of action, and products formed.";
RL J. Biol. Chem. 286:3520-3530(2011).
CC -!- FUNCTION: Catalyzes the formation of branch points in alpha-glucans by
CC cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the
CC cleaved-off oligosaccharide to a new alpha-1,6 position. The branch
CC chain-length distribution of the reaction products shows degree of
CC polymerization (DP) of 3 to 13, with two local maxima at DP 7 and DP
CC 11. Exhibits an alpha-retaining catalytic mechanism. Is involved in
CC glycogen biosynthesis. Shows a secondary activity, i.e. the hydrolysis
CC of the substrate, being 4% of the total activity. Can use amylose as
CC substrate but not alpha-1,4-linked oligosaccharides of 2-7 glucose
CC residues, beta-cyclodextrin, 6-O-glucosyl-beta-cyclodextrin and 6-O-
CC maltosyl-beta-cyclodextrin. Is not able to branch amylopectin further,
CC it only hydrolyzes amylopectin. Thus, displays preference for linear
CC and long substrates (amylose) over branched structures (amylopectin).
CC {ECO:0000269|PubMed:21097495}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a
CC primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
CC Evidence={ECO:0000269|PubMed:21097495};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:21097495};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. Remains fully active
CC following incubation for 1 hour at 80 degrees Celsius.
CC {ECO:0000269|PubMed:21097495};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000269|PubMed:21097495}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family. {ECO:0000305}.
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DR EMBL; AP008226; BAD71725.1; -; Genomic_DNA.
DR RefSeq; WP_011228999.1; NC_006461.1.
DR RefSeq; YP_145168.1; NC_006461.1.
DR PDB; 1UFA; X-ray; 2.20 A; A=1-520.
DR PDB; 3P0B; X-ray; 1.35 A; A=1-520.
DR PDBsum; 1UFA; -.
DR PDBsum; 3P0B; -.
DR AlphaFoldDB; Q5SH28; -.
DR SMR; Q5SH28; -.
DR STRING; 300852.55773284; -.
DR CAZy; GH57; Glycoside Hydrolase Family 57.
DR EnsemblBacteria; BAD71725; BAD71725; BAD71725.
DR GeneID; 3167991; -.
DR KEGG; ttj:TTHA1902; -.
DR PATRIC; fig|300852.9.peg.1870; -.
DR eggNOG; COG1543; Bacteria.
DR HOGENOM; CLU_008192_1_0_0; -.
DR OMA; CAYYEGL; -.
DR PhylomeDB; Q5SH28; -.
DR UniPathway; UPA00164; -.
DR EvolutionaryTrace; Q5SH28; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IDA:UniProtKB.
DR GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC.
DR GO; GO:0030979; P:alpha-glucan biosynthetic process; IEA:InterPro.
DR GO; GO:0005978; P:glycogen biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.20.1430.10; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR037090; 57_glycoside_trans_central.
DR InterPro; IPR015293; BE_C.
DR InterPro; IPR040042; Branching_enz_MT3115-like.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR004300; Glyco_hydro_57_N.
DR PANTHER; PTHR41695; PTHR41695; 1.
DR Pfam; PF09210; DUF1957; 1.
DR Pfam; PF03065; Glyco_hydro_57; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycogen biosynthesis;
KW Glycogen metabolism; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..520
FT /note="1,4-alpha-glucan branching enzyme TTHA1902"
FT /id="PRO_0000413974"
FT ACT_SITE 184
FT /note="Nucleophile"
FT ACT_SITE 353
FT /note="Proton donor"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 236
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MUTAGEN 23
FT /note="F->A: Nearly no effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:21097495"
FT MUTAGEN 184
FT /note="E->A: Complete loss of enzymatic activity. Binds
FT amylose but not glycogen."
FT /evidence="ECO:0000269|PubMed:21097495"
FT MUTAGEN 236
FT /note="Y->A: Almost complete loss of branching activity but
FT 10-fold increase in hydrolytic activity."
FT /evidence="ECO:0000269|PubMed:21097495"
FT MUTAGEN 271
FT /note="L->A: Nearly no effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:21097495"
FT MUTAGEN 274
FT /note="W->A: 0.4% of wild-type enzymatic activity."
FT /evidence="ECO:0000269|PubMed:21097495"
FT MUTAGEN 353
FT /note="D->A: Complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:21097495"
FT MUTAGEN 360
FT /note="W->A: 0.6% of wild-type enzymatic activity."
FT /evidence="ECO:0000269|PubMed:21097495"
FT MUTAGEN 404
FT /note="W->A: 0.4% of wild-type enzymatic activity."
FT /evidence="ECO:0000269|PubMed:21097495"
FT MUTAGEN 463
FT /note="F->A: 0.5% of wild-type enzymatic activity."
FT /evidence="ECO:0000269|PubMed:21097495"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 70..94
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 100..119
FT /evidence="ECO:0007829|PDB:3P0B"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 155..173
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:3P0B"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:3P0B"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 318..342
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:3P0B"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 364..375
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:3P0B"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:3P0B"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 419..438
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 443..456
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:3P0B"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:3P0B"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 471..490
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 494..503
FT /evidence="ECO:0007829|PDB:3P0B"
FT HELIX 512..516
FT /evidence="ECO:0007829|PDB:3P0B"
SQ SEQUENCE 520 AA; 59169 MW; 7B9C8668C760E259 CRC64;
MARFALVLHA HLPYVRAHGM WPFGEETLYE AMAETYLPLI RVLERLRAEG VEAPFTLGIT
PILAEQLADA RIKEGFWAYA KDRLERAQGD YQRYRGTALE ASARHQVAFW ELTLDHFQRL
SGDLVAAFRK AEEGGQVELI TSNATHGYSP LLGYDEALWA QIKTGVSTYR RHFAKDPTGF
WLPEMAYRPK GPWKPPVEGP PEGVRPGVDE LLMRAGIRYT FVDAHLVQGG EPLSPYGEAA
LGPVESQEAT YHVHELESGL RVLARNPETT LQVWSADYGY PGEGLYREFH RKDPLSGLHH
WRVTHRKADL AEKAPYDPEA AFAKTEEHAR HFVGLLERLA GRHPEGVILS PYDAELFGHW
WYEGVAWLEA VLRLLAQNPK VRPVTAREAV QGPAVRTALP EGSWGRGGDH RVWLNEKTLD
YWEKVYRAEG AMREAARRGV LPEGVLRQAM RELLLLEASD WPFLMETGQA EAYARERYEE
HARAFFHLLK GASPEELRAL EERDNPFPEA DPRLYLFREA
