Q5SH28 (BE_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1,4-alpha-glucan branching enzyme TTHA1902
EC=2.4.1.18

Alternative name(s):
1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase
Alpha-(1->4)-glucan branching enzyme
Branching enzyme
Short name=BE

Gene names

Ordered Locus Names:	TTHA1902
ORF Names:	TT1467

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 3 to 13, with two local maxima at DP 7 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Is involved in glycogen biosynthesis. Shows a secondary activity, i.e. the hydrolysis of the substrate, being 4% of the total activity. Can use amylose as substrate but not alpha-1,4-linked oligosaccharides of 2-7 glucose residues, beta-cyclodextrin, 6-O-glucosyl-beta-cyclodextrin and 6-O-maltosyl-beta-cyclodextrin. Is not able to branch amylopectin further, it only hydrolyzes amylopectin. Thus, displays preference for linear and long substrates (amylose) over branched structures (amylopectin). Ref.3
Catalytic activity	Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain. Ref.3
Pathway	Glycan biosynthesis; glycogen biosynthesis. Ref.3
Sequence similarities	Belongs to the glycosyl hydrolase 57 family.
Biophysicochemical properties	pH dependence: Optimum pH is 6.5. Ref.3 Temperature dependence: Optimum temperature is 65 degrees Celsius. Remains fully active following incubation for 1 hour at 80 degrees Celsius.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen biosynthesis Glycogen metabolism
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycogen biosynthetic process Inferred from direct assay Ref.3. Source: UniProtKB
Molecular_function	1,4-alpha-glucan branching enzyme activity Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 520

520

1,4-alpha-glucan branching enzyme TTHA1902

PRO_0000413974

Sites

Active site

184

1

Nucleophile

Active site

353

1

Proton donor

Binding site

265

1

Substrate By similarity

Binding site

282

1

Substrate; via amide nitrogen By similarity

Binding site

404

1

Substrate By similarity

Binding site

460

1

Substrate By similarity

Binding site

469

1

Substrate By similarity

Site

236

1

Transition state stabilizer By similarity

Experimental info

Mutagenesis

23

1

F → A: Nearly no effect on enzymatic activity. Ref.3

Mutagenesis

184

1

E → A: Complete loss of enzymatic activity. Binds amylose but not glycogen. Ref.3

Mutagenesis

236

1

Y → A: Almost complete loss of branching activity but 10-fold increase in hydrolytic activity. Ref.3

Mutagenesis

271

1

L → A: Nearly no effect on enzymatic activity. Ref.3

Mutagenesis

274

1

W → A: 0.4% of wild-type enzymatic activity. Ref.3

Mutagenesis

353

1

D → A: Complete loss of enzymatic activity. Ref.3

Mutagenesis

360

1

W → A: 0.6% of wild-type enzymatic activity. Ref.3

Mutagenesis

404

1

W → A: 0.4% of wild-type enzymatic activity. Ref.3

Mutagenesis

463

1

F → A: 0.5% of wild-type enzymatic activity. Ref.3

Secondary structure

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520

Helix Strand Turn

Details...

Beta strand

2 – 10

9

Beta strand

20 – 24

5

Helix

25 – 34

10

Helix

36 – 49

14

Beta strand

55 – 59

5

Helix

61 – 67

7

Helix

70 – 94

25

Helix

100 – 119

20

Turn

120 – 122

3

Helix

124 – 133

10

Beta strand

136 – 142

7

Helix

149 – 151

3

Helix

155 – 173

19

Beta strand

179 – 181

3

Helix

183 – 185

3

Beta strand

190 – 193

4

Beta strand

196 – 198

3

Beta strand

203 – 205

3

Helix

208 – 214

7

Beta strand

219 – 222

4

Helix

225 – 228

4

Helix

248 – 251

4

Beta strand

252 – 255

4

Beta strand

261 – 265

5

Helix

267 – 274

8

Turn

276 – 278

3

Helix

280 – 282

3

Turn

294 – 296

3

Helix

310 – 312

3

Helix

318 – 342

25

Beta strand

347 – 353

7

Helix

354 – 356

3

Turn

358 – 360

3

Helix

364 – 375

12

Beta strand

379 – 383

5

Helix

386 – 389

4

Beta strand

394 – 396

3

Helix

406 – 408

3

Turn

411 – 413

3

Helix

416 – 418

3

Helix

419 – 438

20

Helix

443 – 456

14

Helix

460 – 463

4

Turn

464 – 466

3

Turn

468 – 470

3

Helix

471 – 490

20

Helix

494 – 503

10

Helix

512 – 516

5

Sequences

	Sequence		Length	Mass (Da)
	Q5SH28 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 7B9C8668C760E259	FASTA	520	59,169
	10 20 30 40 50 60 MARFALVLHA HLPYVRAHGM WPFGEETLYE AMAETYLPLI RVLERLRAEG VEAPFTLGIT 70 80 90 100 110 120 PILAEQLADA RIKEGFWAYA KDRLERAQGD YQRYRGTALE ASARHQVAFW ELTLDHFQRL 130 140 150 160 170 180 SGDLVAAFRK AEEGGQVELI TSNATHGYSP LLGYDEALWA QIKTGVSTYR RHFAKDPTGF 190 200 210 220 230 240 WLPEMAYRPK GPWKPPVEGP PEGVRPGVDE LLMRAGIRYT FVDAHLVQGG EPLSPYGEAA 250 260 270 280 290 300 LGPVESQEAT YHVHELESGL RVLARNPETT LQVWSADYGY PGEGLYREFH RKDPLSGLHH 310 320 330 340 350 360 WRVTHRKADL AEKAPYDPEA AFAKTEEHAR HFVGLLERLA GRHPEGVILS PYDAELFGHW 370 380 390 400 410 420 WYEGVAWLEA VLRLLAQNPK VRPVTAREAV QGPAVRTALP EGSWGRGGDH RVWLNEKTLD 430 440 450 460 470 480 YWEKVYRAEG AMREAARRGV LPEGVLRQAM RELLLLEASD WPFLMETGQA EAYARERYEE 490 500 510 520 HARAFFHLLK GASPEELRAL EERDNPFPEA DPRLYLFREA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579.
[2]	"Crystal structure of TT1467 from Thermus thermophilus HB8." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS). Strain: HB8 / ATCC 27634 / DSM 579.
[3]	"Thermus thermophilus glycoside hydrolase family 57 branching enzyme: crystal structure, mechanism of action, and products formed." Palomo M., Pijning T., Booiman T., Dobruchowska J.M., van der Vlist J., Kralj S., Planas A., Loos K., Kamerling J.P., Dijkstra B.W., van der Maarel M.J., Dijkhuizen L., Leemhuis H. J. Biol. Chem. 286:3520-3530(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, MUTAGENESIS OF PHE-23; GLU-184; TYR-236; LEU-271; TRP-274; ASP-353; TRP-360; TRP-404 AND PHE-463. Strain: HB8 / ATCC 27634 / DSM 579.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP008226 Genomic DNA. Translation: BAD71725.1.

RefSeq

YP_145168.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UFA	X-ray	2.20	A	1-520	[»]
3P0B	X-ray	1.35	A	1-520	[»]

ProteinModelPortal

Q5SH28.

SMR

Q5SH28. Positions 1-517.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1902.

Protein family/group databases

CAZy

GH57. Glycoside Hydrolase Family 57.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71725; BAD71725; BAD71725.

GeneID

3167991.

KEGG

ttj:TTHA1902.

PATRIC

23958769. VBITheThe93045_1870.

Phylogenomic databases

eggNOG

COG1543.

HOGENOM

HOG000046905.

OMA

EAITETY.

ProtClustDB

CLSK434192.

Enzyme and pathway databases

UniPathway

UPA00164.

Family and domain databases

Gene3D

1.20.1430.10. 1 hit.
3.20.110.10. 1 hit.

InterPro

IPR015293. DUF1957.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR027291. Glyco_hydro_38/57_N.
IPR004300. Glyco_hydro_57_N.
[Graphical view]

Pfam

PF09210. DUF1957. 1 hit.
PF03065. Glyco_hydro_57. 1 hit.
[Graphical view]

SUPFAM

SSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q5SH28.

Entry information

Entry name

BE_THET8

Accession

Primary (citable) accession number: Q5SH28
Secondary accession number(s): P84162

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2011
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program