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Q5JDJ7

- BE_THEKO

UniProt

Q5JDJ7 - BE_THEKO

Protein

1,4-alpha-glucan branching enzyme TK1436

Gene

TK1436

Organism
Thermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
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    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 5 to 30, with two local maxima at DP 6 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Does not display alpha-galactosidase or pullulanase activity, since melibiose and pullulan are not substrates. Is not able to catalyze the hydrolysis or transglycosylation of maltoheptaose, suggesting that the TK1436 protein contains neither alpha-amylase nor 4-alpha-glucanotransferase activity.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 7.0.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius. Is thermostable up to 90 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei183 – 1831Nucleophile1 Publication
    Sitei233 – 2331Transition state stabilizerCurated
    Binding sitei261 – 2611Substrate
    Binding sitei278 – 2781Substrate; via amide nitrogen
    Active sitei354 – 3541Proton donor1 Publication
    Binding sitei407 – 4071Substrate
    Binding sitei467 – 4671Substrate
    Binding sitei476 – 4761Substrate

    GO - Molecular functioni

    1. 1,4-alpha-glucan branching enzyme activity Source: UniProtKB
    2. DNA binding Source: InterPro
    3. nucleotide binding Source: InterPro

    GO - Biological processi

    1. alpha-glucan biosynthetic process Source: UniProtKB
    2. DNA repair Source: InterPro

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    BioCyciTKOD69014:GH72-1461-MONOMER.
    BRENDAi2.4.1.18. 264868.

    Protein family/group databases

    CAZyiGH57. Glycoside Hydrolase Family 57.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1,4-alpha-glucan branching enzyme TK1436 (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:TK1436
    OrganismiThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
    Taxonomic identifieri69014 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
    ProteomesiUP000000536: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6756751,4-alpha-glucan branching enzyme TK1436PRO_0000413973Add
    BLAST

    Expressioni

    Inductioni

    Up-regulated by maltodextrin.1 Publication

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    STRINGi69014.TK1436.

    Structurei

    Secondary structure

    1
    675
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 118
    Beta strandi22 – 254
    Helixi26 – 3510
    Helixi37 – 4913
    Beta strandi56 – 605
    Helixi62 – 687
    Helixi71 – 9424
    Helixi99 – 11820
    Turni119 – 1213
    Helixi123 – 13210
    Beta strandi135 – 1417
    Helixi148 – 1503
    Helixi154 – 17219
    Beta strandi177 – 1804
    Helixi182 – 1843
    Beta strandi189 – 1935
    Helixi195 – 1973
    Beta strandi199 – 2024
    Helixi205 – 2106
    Turni211 – 2133
    Beta strandi216 – 2194
    Helixi221 – 2255
    Beta strandi231 – 2344
    Beta strandi245 – 2473
    Beta strandi249 – 2513
    Beta strandi257 – 2604
    Helixi263 – 2708
    Turni272 – 2743
    Helixi276 – 2783
    Turni290 – 2923
    Beta strandi301 – 3044
    Helixi306 – 3083
    Helixi314 – 34330
    Beta strandi348 – 3547
    Helixi355 – 3573
    Turni359 – 3613
    Helixi365 – 37814
    Helixi386 – 3916
    Beta strandi398 – 4003
    Helixi409 – 4113
    Turni414 – 4163
    Turni419 – 4235
    Helixi424 – 44219
    Helixi447 – 46317
    Helixi467 – 4737
    Helixi478 – 50528
    Helixi510 – 51910
    Helixi529 – 5313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3N8TX-ray2.40A1-562[»]
    3N92X-ray2.89A1-562[»]
    3N98X-ray1.87A1-562[»]
    ProteinModelPortaliQ5JDJ7.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5JDJ7.

    Family & Domainsi

    Domaini

    The C-terminus contains two copies of a helix-hairpin-helix (HhH) motif that are dispensable for activity and thermal stability.1 Publication

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 57 family.Curated

    Phylogenomic databases

    eggNOGiCOG1543.
    HOGENOMiHOG000046905.
    OMAiAFFGRDS.

    Family and domain databases

    Gene3Di1.20.1430.10. 1 hit.
    3.20.110.10. 1 hit.
    InterProiIPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
    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.
    IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
    [Graphical view]
    PfamiPF09210. DUF1957. 1 hit.
    PF03065. Glyco_hydro_57. 1 hit.
    [Graphical view]
    SMARTiSM00278. HhH1. 2 hits.
    [Graphical view]
    SUPFAMiSSF47794. SSF47794. 1 hit.
    SSF88688. SSF88688. 1 hit.
    SSF88713. SSF88713. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q5JDJ7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGYLTFVLH THIPYVRKHG KWPFGEEWVF EAISETYIPL LMEFERLRDS    50
    GVKFGIVINV TPVLAEQLTD EYMKKAFEEY MERKLKAMEE DLKSGKYDEK 100
    AVSYMLNYFR KVYDYWKAIN GDIIGKLREL QDQGYVEVIT SAATHGYLPL 150
    LGRDEAIRAQ IANGVATYEK HFGMKPKGIW LPECAYRPAG EWELPGGRKV 200
    KRQGIEKFLE EFGLRYFFVE SRLIDEGPAS NVYGEVLIAD TEKTTLRPYW 250
    IKGSNVAVFA RNRETGHQVW SAHYGYPGDF WYREFHKKAP KSGGQYWRIT 300
    SKEVGLGEKE FYDPDKAMER VEEHARHFVS LVERLLREHE EKFGEKGIIV 350
    APYDTELFGH WWFEGVKWLG RVLELLYQRG VETPTLSRFL EEYSGEKHEI 400
    ELPEGSWGAN SDHSTWWNEE TEWTWPHIYR AEDRMVAIVS RFRGRDELTN 450
    RVIEQLAREL LILEASDWQF LITTGQAKEY AKRRVLIHSR DFHRLANELV 500
    RYVKIGEFDV KLLEELEERD NPFRPVVVGP YVSENPPELE EYVEPPEVPP 550
    EKEETEEKPK VLTEKATSLA LAVKKVKPVK EETREVKKKA VEASKRGKRK 600
    SSKSKRLPRK VSKKAPSKGP SDLLSIKGIG PKTFQKLKRA GVETIEDLKN 650
    ANIEDLARKT GISTKRLKKF IAQVE 675
    Length:675
    Mass (Da):78,549
    Last modified:February 15, 2005 - v1
    Checksum:i857E34E04F23B27A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006878 Genomic DNA. Translation: BAD85625.1.
    RefSeqiYP_183849.1. NC_006624.1.

    Genome annotation databases

    EnsemblBacteriaiBAD85625; BAD85625; TK1436.
    GeneIDi3234278.
    KEGGitko:TK1436.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006878 Genomic DNA. Translation: BAD85625.1 .
    RefSeqi YP_183849.1. NC_006624.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3N8T X-ray 2.40 A 1-562 [» ]
    3N92 X-ray 2.89 A 1-562 [» ]
    3N98 X-ray 1.87 A 1-562 [» ]
    ProteinModelPortali Q5JDJ7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 69014.TK1436.

    Protein family/group databases

    CAZyi GH57. Glycoside Hydrolase Family 57.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD85625 ; BAD85625 ; TK1436 .
    GeneIDi 3234278.
    KEGGi tko:TK1436.

    Phylogenomic databases

    eggNOGi COG1543.
    HOGENOMi HOG000046905.
    OMAi AFFGRDS.

    Enzyme and pathway databases

    BioCyci TKOD69014:GH72-1461-MONOMER.
    BRENDAi 2.4.1.18. 264868.

    Miscellaneous databases

    EvolutionaryTracei Q5JDJ7.

    Family and domain databases

    Gene3Di 1.20.1430.10. 1 hit.
    3.20.110.10. 1 hit.
    InterProi IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
    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.
    IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
    [Graphical view ]
    Pfami PF09210. DUF1957. 1 hit.
    PF03065. Glyco_hydro_57. 1 hit.
    [Graphical view ]
    SMARTi SM00278. HhH1. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47794. SSF47794. 1 hit.
    SSF88688. SSF88688. 1 hit.
    SSF88713. SSF88713. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
      Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
      Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-918 / JCM 12380 / KOD1.
    2. "A novel branching enzyme of the GH-57 family in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1."
      Murakami T., Kanai T., Takata H., Kuriki T., Imanaka T.
      J. Bacteriol. 188:5915-5924(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, SUBUNIT, DOMAIN.
      Strain: ATCC BAA-918 / JCM 12380 / KOD1.
    3. "Structural basis for branching-enzyme activity of glycoside hydrolase family 57: structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1."
      Santos C.R., Tonoli C.C., Trindade D.M., Betzel C., Takata H., Kuriki T., Kanai T., Imanaka T., Arni R.K., Murakami M.T.
      Proteins 79:547-557(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 1-562 OF APOENZYME AND IN COMPLEXES WITH GLUCOSE AND SUBSTRATE ANALOGS, SUBUNIT, ACTIVE SITES.
      Strain: ATCC BAA-918 / JCM 12380 / KOD1.

    Entry informationi

    Entry nameiBE_THEKO
    AccessioniPrimary (citable) accession number: Q5JDJ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2011
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 66 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3