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Protein

1,4-alpha-glucan branching enzyme TTHA1902

Gene

TTHA1902

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: 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.1 Publication

Pathwayi: glycogen biosynthesis

This protein is involved in the pathway glycogen biosynthesis, which is part of Glycan biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway glycogen biosynthesis and in Glycan biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei184Nucleophile1
Sitei236Transition state stabilizerBy similarity1
Binding sitei265SubstrateBy similarity1
Binding sitei282Substrate; via amide nitrogenBy similarity1
Active sitei353Proton donor1
Binding sitei404SubstrateBy similarity1
Binding sitei460SubstrateBy similarity1
Binding sitei469SubstrateBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • 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-1891-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
Proteomesi
  • UP000000532 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23F → A: Nearly no effect on enzymatic activity. 1 Publication1
Mutagenesisi184E → A: Complete loss of enzymatic activity. Binds amylose but not glycogen. 1 Publication1
Mutagenesisi236Y → A: Almost complete loss of branching activity but 10-fold increase in hydrolytic activity. 1 Publication1
Mutagenesisi271L → A: Nearly no effect on enzymatic activity. 1 Publication1
Mutagenesisi274W → A: 0.4% of wild-type enzymatic activity. 1 Publication1
Mutagenesisi353D → A: Complete loss of enzymatic activity. 1 Publication1
Mutagenesisi360W → A: 0.6% of wild-type enzymatic activity. 1 Publication1
Mutagenesisi404W → A: 0.4% of wild-type enzymatic activity. 1 Publication1
Mutagenesisi463F → A: 0.5% of wild-type enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004139741 – 5201,4-alpha-glucan branching enzyme TTHA1902Add BLAST520

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA1902.

Structurei

Secondary structure

1520
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 10Combined sources9
Beta strandi20 – 24Combined sources5
Helixi25 – 34Combined sources10
Helixi36 – 49Combined sources14
Beta strandi55 – 59Combined sources5
Helixi61 – 67Combined sources7
Helixi70 – 94Combined sources25
Helixi100 – 119Combined sources20
Turni120 – 122Combined sources3
Helixi124 – 133Combined sources10
Beta strandi136 – 142Combined sources7
Helixi149 – 151Combined sources3
Helixi155 – 173Combined sources19
Beta strandi179 – 181Combined sources3
Helixi183 – 185Combined sources3
Beta strandi190 – 193Combined sources4
Beta strandi196 – 198Combined sources3
Beta strandi203 – 205Combined sources3
Helixi208 – 214Combined sources7
Beta strandi219 – 222Combined sources4
Helixi225 – 228Combined sources4
Helixi248 – 251Combined sources4
Beta strandi252 – 255Combined sources4
Beta strandi261 – 265Combined sources5
Helixi267 – 274Combined sources8
Turni276 – 278Combined sources3
Helixi280 – 282Combined sources3
Turni294 – 296Combined sources3
Helixi310 – 312Combined sources3
Helixi318 – 342Combined sources25
Beta strandi347 – 353Combined sources7
Helixi354 – 356Combined sources3
Turni358 – 360Combined sources3
Helixi364 – 375Combined sources12
Beta strandi379 – 383Combined sources5
Helixi386 – 389Combined sources4
Beta strandi394 – 396Combined sources3
Helixi406 – 408Combined sources3
Turni411 – 413Combined sources3
Helixi416 – 418Combined sources3
Helixi419 – 438Combined sources20
Helixi443 – 456Combined sources14
Helixi460 – 463Combined sources4
Turni464 – 466Combined sources3
Turni468 – 470Combined sources3
Helixi471 – 490Combined sources20
Helixi494 – 503Combined sources10
Helixi512 – 516Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UFAX-ray2.20A1-520[»]
3P0BX-ray1.35A1-520[»]
ProteinModelPortaliQ5SH28.
SMRiQ5SH28.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SH28.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 57 family.Curated

Phylogenomic databases

eggNOGiENOG4107RFW. Bacteria.
COG1543. LUCA.
HOGENOMiHOG000046905.
KOiK16149.
OMAiPECAYYE.

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

« Hide

        10         20         30         40         50
MARFALVLHA HLPYVRAHGM WPFGEETLYE AMAETYLPLI RVLERLRAEG
60 70 80 90 100
VEAPFTLGIT PILAEQLADA RIKEGFWAYA KDRLERAQGD YQRYRGTALE
110 120 130 140 150
ASARHQVAFW ELTLDHFQRL SGDLVAAFRK AEEGGQVELI TSNATHGYSP
160 170 180 190 200
LLGYDEALWA QIKTGVSTYR RHFAKDPTGF WLPEMAYRPK GPWKPPVEGP
210 220 230 240 250
PEGVRPGVDE LLMRAGIRYT FVDAHLVQGG EPLSPYGEAA LGPVESQEAT
260 270 280 290 300
YHVHELESGL RVLARNPETT LQVWSADYGY PGEGLYREFH RKDPLSGLHH
310 320 330 340 350
WRVTHRKADL AEKAPYDPEA AFAKTEEHAR HFVGLLERLA GRHPEGVILS
360 370 380 390 400
PYDAELFGHW WYEGVAWLEA VLRLLAQNPK VRPVTAREAV QGPAVRTALP
410 420 430 440 450
EGSWGRGGDH RVWLNEKTLD YWEKVYRAEG AMREAARRGV LPEGVLRQAM
460 470 480 490 500
RELLLLEASD WPFLMETGQA EAYARERYEE HARAFFHLLK GASPEELRAL
510 520
EERDNPFPEA DPRLYLFREA
Length:520
Mass (Da):59,169
Last modified:December 21, 2004 - v1
Checksum:i7B9C8668C760E259
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71725.1.
RefSeqiWP_011228999.1. NC_006461.1.
YP_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:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71725.1.
RefSeqiWP_011228999.1. NC_006461.1.
YP_145168.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UFAX-ray2.20A1-520[»]
3P0BX-ray1.35A1-520[»]
ProteinModelPortaliQ5SH28.
SMRiQ5SH28.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1902.

Protein family/group databases

CAZyiGH57. Glycoside Hydrolase Family 57.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4107RFW. Bacteria.
COG1543. LUCA.
HOGENOMiHOG000046905.
KOiK16149.
OMAiPECAYYE.

Enzyme and pathway databases

UniPathwayiUPA00164.
BioCyciTTHE300852:GH8R-1891-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SH28.

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.
ProtoNetiSearch...

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: November 2, 2016
This is version 65 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.