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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiQ5JDJ7.
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

        10         20         30         40         50
MKGYLTFVLH THIPYVRKHG KWPFGEEWVF EAISETYIPL LMEFERLRDS
60 70 80 90 100
GVKFGIVINV TPVLAEQLTD EYMKKAFEEY MERKLKAMEE DLKSGKYDEK
110 120 130 140 150
AVSYMLNYFR KVYDYWKAIN GDIIGKLREL QDQGYVEVIT SAATHGYLPL
160 170 180 190 200
LGRDEAIRAQ IANGVATYEK HFGMKPKGIW LPECAYRPAG EWELPGGRKV
210 220 230 240 250
KRQGIEKFLE EFGLRYFFVE SRLIDEGPAS NVYGEVLIAD TEKTTLRPYW
260 270 280 290 300
IKGSNVAVFA RNRETGHQVW SAHYGYPGDF WYREFHKKAP KSGGQYWRIT
310 320 330 340 350
SKEVGLGEKE FYDPDKAMER VEEHARHFVS LVERLLREHE EKFGEKGIIV
360 370 380 390 400
APYDTELFGH WWFEGVKWLG RVLELLYQRG VETPTLSRFL EEYSGEKHEI
410 420 430 440 450
ELPEGSWGAN SDHSTWWNEE TEWTWPHIYR AEDRMVAIVS RFRGRDELTN
460 470 480 490 500
RVIEQLAREL LILEASDWQF LITTGQAKEY AKRRVLIHSR DFHRLANELV
510 520 530 540 550
RYVKIGEFDV KLLEELEERD NPFRPVVVGP YVSENPPELE EYVEPPEVPP
560 570 580 590 600
EKEETEEKPK VLTEKATSLA LAVKKVKPVK EETREVKKKA VEASKRGKRK
610 620 630 640 650
SSKSKRLPRK VSKKAPSKGP SDLLSIKGIG PKTFQKLKRA GVETIEDLKN
660 670
ANIEDLARKT GISTKRLKKF IAQVE
Length:675
Mass (Da):78,549
Last modified:February 15, 2005 - v1
Checksum:i857E34E04F23B27A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AP006878 Genomic DNA. Translation: BAD85625.1 .
RefSeqi YP_183849.1. NC_006624.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi Q5JDJ7.
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: November 26, 2014
This is version 68 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