BE_THEKO
ID BE_THEKO Reviewed; 675 AA.
AC Q5JDJ7;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=1,4-alpha-glucan branching enzyme TK1436;
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=TK1436;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=16885460; DOI=10.1128/jb.00390-06;
RA Murakami T., Kanai T., Takata H., Kuriki T., Imanaka T.;
RT "A novel branching enzyme of the GH-57 family in the hyperthermophilic
RT archaeon Thermococcus kodakaraensis KOD1.";
RL J. Bacteriol. 188:5915-5924(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 1-562 OF APOENZYME AND IN
RP COMPLEXES WITH GLUCOSE AND SUBSTRATE ANALOGS, SUBUNIT, AND ACTIVE SITES.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=21104698; DOI=10.1002/prot.22902;
RA Santos C.R., Tonoli C.C., Trindade D.M., Betzel C., Takata H., Kuriki T.,
RA Kanai T., Imanaka T., Arni R.K., Murakami M.T.;
RT "Structural basis for branching-enzyme activity of glycoside hydrolase
RT family 57: structure and stability studies of a novel branching enzyme from
RT the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1.";
RL Proteins 79:547-557(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 5 to 30, with two local maxima at DP 6 and DP
CC 11. Exhibits an alpha-retaining catalytic mechanism. Does not display
CC alpha-galactosidase or pullulanase activity, since melibiose and
CC pullulan are not substrates. Is not able to catalyze the hydrolysis or
CC transglycosylation of maltoheptaose, suggesting that the TK1436 protein
CC contains neither alpha-amylase nor 4-alpha-glucanotransferase activity.
CC {ECO:0000269|PubMed:16885460}.
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:16885460};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:16885460};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Is thermostable up to 90
CC degrees Celsius. {ECO:0000269|PubMed:16885460};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16885460,
CC ECO:0000269|PubMed:21104698}.
CC -!- INDUCTION: Up-regulated by maltodextrin. {ECO:0000269|PubMed:16885460}.
CC -!- DOMAIN: The C-terminus contains two copies of a helix-hairpin-helix
CC (HhH) motif that are dispensable for activity and thermal stability.
CC {ECO:0000269|PubMed:16885460}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family. {ECO:0000305}.
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DR EMBL; AP006878; BAD85625.1; -; Genomic_DNA.
DR RefSeq; WP_011250387.1; NC_006624.1.
DR PDB; 3N8T; X-ray; 2.40 A; A=1-562.
DR PDB; 3N92; X-ray; 2.89 A; A=1-562.
DR PDB; 3N98; X-ray; 1.87 A; A=1-562.
DR PDBsum; 3N8T; -.
DR PDBsum; 3N92; -.
DR PDBsum; 3N98; -.
DR AlphaFoldDB; Q5JDJ7; -.
DR SMR; Q5JDJ7; -.
DR STRING; 69014.TK1436; -.
DR CAZy; GH57; Glycoside Hydrolase Family 57.
DR EnsemblBacteria; BAD85625; BAD85625; TK1436.
DR GeneID; 3234278; -.
DR KEGG; tko:TK1436; -.
DR PATRIC; fig|69014.16.peg.1398; -.
DR eggNOG; arCOG03281; Archaea.
DR HOGENOM; CLU_008192_1_0_2; -.
DR InParanoid; Q5JDJ7; -.
DR OMA; CAYYEGL; -.
DR OrthoDB; 4556at2157; -.
DR PhylomeDB; Q5JDJ7; -.
DR BRENDA; 2.4.1.18; 5246.
DR EvolutionaryTrace; Q5JDJ7; -.
DR Proteomes; UP000000536; 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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0030979; P:alpha-glucan 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; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
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; SSF47794; SSF47794; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..675
FT /note="1,4-alpha-glucan branching enzyme TK1436"
FT /id="PRO_0000413973"
FT REGION 537..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..613
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:21104698"
FT ACT_SITE 354
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:21104698"
FT BINDING 261
FT /ligand="substrate"
FT BINDING 278
FT /ligand="substrate"
FT BINDING 407
FT /ligand="substrate"
FT BINDING 467
FT /ligand="substrate"
FT BINDING 476
FT /ligand="substrate"
FT SITE 233
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 71..94
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 99..118
FT /evidence="ECO:0007829|PDB:3N98"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 154..172
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:3N98"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:3N92"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:3N98"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3N98"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 314..343
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:3N98"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 365..378
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 386..391
FT /evidence="ECO:0007829|PDB:3N98"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:3N98"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:3N98"
FT TURN 419..423
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 424..442
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 447..463
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 467..473
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 478..505
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 510..519
FT /evidence="ECO:0007829|PDB:3N98"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:3N98"
SQ SEQUENCE 675 AA; 78549 MW; 857E34E04F23B27A CRC64;
MKGYLTFVLH THIPYVRKHG KWPFGEEWVF EAISETYIPL LMEFERLRDS GVKFGIVINV
TPVLAEQLTD EYMKKAFEEY MERKLKAMEE DLKSGKYDEK AVSYMLNYFR KVYDYWKAIN
GDIIGKLREL QDQGYVEVIT SAATHGYLPL LGRDEAIRAQ IANGVATYEK HFGMKPKGIW
LPECAYRPAG EWELPGGRKV KRQGIEKFLE EFGLRYFFVE SRLIDEGPAS NVYGEVLIAD
TEKTTLRPYW IKGSNVAVFA RNRETGHQVW SAHYGYPGDF WYREFHKKAP KSGGQYWRIT
SKEVGLGEKE FYDPDKAMER VEEHARHFVS LVERLLREHE EKFGEKGIIV APYDTELFGH
WWFEGVKWLG RVLELLYQRG VETPTLSRFL EEYSGEKHEI ELPEGSWGAN SDHSTWWNEE
TEWTWPHIYR AEDRMVAIVS RFRGRDELTN RVIEQLAREL LILEASDWQF LITTGQAKEY
AKRRVLIHSR DFHRLANELV RYVKIGEFDV KLLEELEERD NPFRPVVVGP YVSENPPELE
EYVEPPEVPP EKEETEEKPK VLTEKATSLA LAVKKVKPVK EETREVKKKA VEASKRGKRK
SSKSKRLPRK VSKKAPSKGP SDLLSIKGIG PKTFQKLKRA GVETIEDLKN ANIEDLARKT
GISTKRLKKF IAQVE
