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Q5JDJ7

- BE_THEKO

UniProt

Q5JDJ7 - BE_THEKO

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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

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei183 – 1831Nucleophile1 Publication
Sitei233 – 2331Transition state stabilizer Inferred
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
Complete GO annotation...

GO - Biological processi

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

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 TK1436
PRO_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

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.

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

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...

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

« Hide 'large scale' publications
  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: June 11, 2014
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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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