Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5SH28

- BE_THET8

UniProt

Q5SH28 - BE_THET8

Protein

1,4-alpha-glucan branching enzyme TTHA1902

Gene

TTHA1902

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycogen biosynthetic process Source: UniProtKB

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SH28.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 57 family.Curated

    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

    « Hide

    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

    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: October 1, 2014
    This is version 53 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