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Q5SH28

- BE_THET8

UniProt

Q5SH28 - BE_THET8

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Protein

1,4-alpha-glucan branching enzyme TTHA1902

Gene
TTHA1902, TT1467
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.1 Publication

pH dependencei

Optimum pH is 6.5.1 Publication

Temperature dependencei

Optimum temperature is 65 degrees Celsius. Remains fully active following incubation for 1 hour at 80 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei184 – 1841Nucleophile
Sitei236 – 2361Transition state stabilizer By similarity
Binding sitei265 – 2651Substrate By similarity
Binding sitei282 – 2821Substrate; via amide nitrogen By similarity
Active sitei353 – 3531Proton donor
Binding sitei404 – 4041Substrate By similarity
Binding sitei460 – 4601Substrate By similarity
Binding sitei469 – 4691Substrate By similarity

GO - Molecular functioni

  1. 1,4-alpha-glucan branching enzyme activity Source: UniProtKB

GO - Biological processi

  1. glycogen biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1948-MONOMER.
UniPathwayiUPA00164.

Protein family/group databases

CAZyiGH57. Glycoside Hydrolase Family 57.

Names & Taxonomyi

Protein namesi
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 namesi
Ordered Locus Names:TTHA1902
ORF Names:TT1467
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231F → A: Nearly no effect on enzymatic activity. 1 Publication
Mutagenesisi184 – 1841E → A: Complete loss of enzymatic activity. Binds amylose but not glycogen. 1 Publication
Mutagenesisi236 – 2361Y → A: Almost complete loss of branching activity but 10-fold increase in hydrolytic activity. 1 Publication
Mutagenesisi271 – 2711L → A: Nearly no effect on enzymatic activity. 1 Publication
Mutagenesisi274 – 2741W → A: 0.4% of wild-type enzymatic activity. 1 Publication
Mutagenesisi353 – 3531D → A: Complete loss of enzymatic activity. 1 Publication
Mutagenesisi360 – 3601W → A: 0.6% of wild-type enzymatic activity. 1 Publication
Mutagenesisi404 – 4041W → A: 0.4% of wild-type enzymatic activity. 1 Publication
Mutagenesisi463 – 4631F → A: 0.5% of wild-type enzymatic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5205201,4-alpha-glucan branching enzyme TTHA1902PRO_0000413974Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA1902.

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109
Beta strandi20 – 245
Helixi25 – 3410
Helixi36 – 4914
Beta strandi55 – 595
Helixi61 – 677
Helixi70 – 9425
Helixi100 – 11920
Turni120 – 1223
Helixi124 – 13310
Beta strandi136 – 1427
Helixi149 – 1513
Helixi155 – 17319
Beta strandi179 – 1813
Helixi183 – 1853
Beta strandi190 – 1934
Beta strandi196 – 1983
Beta strandi203 – 2053
Helixi208 – 2147
Beta strandi219 – 2224
Helixi225 – 2284
Helixi248 – 2514
Beta strandi252 – 2554
Beta strandi261 – 2655
Helixi267 – 2748
Turni276 – 2783
Helixi280 – 2823
Turni294 – 2963
Helixi310 – 3123
Helixi318 – 34225
Beta strandi347 – 3537
Helixi354 – 3563
Turni358 – 3603
Helixi364 – 37512
Beta strandi379 – 3835
Helixi386 – 3894
Beta strandi394 – 3963
Helixi406 – 4083
Turni411 – 4133
Helixi416 – 4183
Helixi419 – 43820
Helixi443 – 45614
Helixi460 – 4634
Turni464 – 4663
Turni468 – 4703
Helixi471 – 49020
Helixi494 – 50310
Helixi512 – 5165

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UFAX-ray2.20A1-520[»]
3P0BX-ray1.35A1-520[»]
ProteinModelPortaliQ5SH28.
SMRiQ5SH28. Positions 1-517.

Miscellaneous databases

EvolutionaryTraceiQ5SH28.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1543.
HOGENOMiHOG000046905.
OMAiAFFGRDS.
OrthoDBiEOG6FNHJ7.

Family and domain databases

Gene3Di1.20.1430.10. 1 hit.
3.20.110.10. 1 hit.
InterProiIPR015293. DUF1957.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR027291. Glyco_hydro_38/57_N.
IPR028995. Glyco_hydro_57/38_cen.
IPR004300. Glyco_hydro_57_N.
[Graphical view]
PfamiPF09210. DUF1957. 1 hit.
PF03065. Glyco_hydro_57. 1 hit.
[Graphical view]
SUPFAMiSSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5SH28-1 [UniParc]FASTAAdd to Basket

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MARFALVLHA HLPYVRAHGM WPFGEETLYE AMAETYLPLI RVLERLRAEG    50
VEAPFTLGIT PILAEQLADA RIKEGFWAYA KDRLERAQGD YQRYRGTALE 100
ASARHQVAFW ELTLDHFQRL SGDLVAAFRK AEEGGQVELI TSNATHGYSP 150
LLGYDEALWA QIKTGVSTYR RHFAKDPTGF WLPEMAYRPK GPWKPPVEGP 200
PEGVRPGVDE LLMRAGIRYT FVDAHLVQGG EPLSPYGEAA LGPVESQEAT 250
YHVHELESGL RVLARNPETT LQVWSADYGY PGEGLYREFH RKDPLSGLHH 300
WRVTHRKADL AEKAPYDPEA AFAKTEEHAR HFVGLLERLA GRHPEGVILS 350
PYDAELFGHW WYEGVAWLEA VLRLLAQNPK VRPVTAREAV QGPAVRTALP 400
EGSWGRGGDH RVWLNEKTLD YWEKVYRAEG AMREAARRGV LPEGVLRQAM 450
RELLLLEASD WPFLMETGQA EAYARERYEE HARAFFHLLK GASPEELRAL 500
EERDNPFPEA DPRLYLFREA 520
Length:520
Mass (Da):59,169
Last modified:December 21, 2004 - v1
Checksum:i7B9C8668C760E259
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD71725.1.
RefSeqiYP_145168.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71725; BAD71725; BAD71725.
GeneIDi3167991.
KEGGittj:TTHA1902.
PATRICi23958769. VBITheThe93045_1870.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD71725.1 .
RefSeqi YP_145168.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UFA X-ray 2.20 A 1-520 [» ]
3P0B X-ray 1.35 A 1-520 [» ]
ProteinModelPortali Q5SH28.
SMRi Q5SH28. Positions 1-517.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA1902.

Protein family/group databases

CAZyi GH57. Glycoside Hydrolase Family 57.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD71725 ; BAD71725 ; BAD71725 .
GeneIDi 3167991.
KEGGi ttj:TTHA1902.
PATRICi 23958769. VBITheThe93045_1870.

Phylogenomic databases

eggNOGi COG1543.
HOGENOMi HOG000046905.
OMAi AFFGRDS.
OrthoDBi EOG6FNHJ7.

Enzyme and pathway databases

UniPathwayi UPA00164 .
BioCyci TTHE300852:GH8R-1948-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q5SH28.

Family and domain databases

Gene3Di 1.20.1430.10. 1 hit.
3.20.110.10. 1 hit.
InterProi IPR015293. DUF1957.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR027291. Glyco_hydro_38/57_N.
IPR028995. Glyco_hydro_57/38_cen.
IPR004300. Glyco_hydro_57_N.
[Graphical view ]
Pfami PF09210. DUF1957. 1 hit.
PF03065. Glyco_hydro_57. 1 hit.
[Graphical view ]
SUPFAMi SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiBE_THET8
AccessioniPrimary (citable) accession number: Q5SH28
Secondary accession number(s): P84162
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: December 21, 2004
Last modified: June 11, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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