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O32462

- MALQ_THELN

UniProt

O32462 - MALQ_THELN

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Protein
4-alpha-glucanotransferase
Gene
jgt, OCC_10078
Organism
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the transglycosylation of maltooligosaccharides, yielding maltooligosaccharides of various lengths and glucose. Maltose and glucose can be used as acceptors in the transfer reaction.1 Publication

Catalytic activityi

Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.1 Publication

Enzyme regulationi

Inhibited by p-chloromercuribenzoic acid, monoiodoacetic acid, mercury and nickel ions.

Kineticsi

    Vmax=13 µmol/min/mg enzyme with maltose as substrate1 Publication

    Vmax=26 µmol/min/mg enzyme with maltotriose as substrate

    Temperature dependencei

    Optimum temperature is 85-100 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei123 – 1231Nucleophile
    Active sitei214 – 2141Proton donor

    GO - Molecular functioni

    1. 4-alpha-glucanotransferase activity Source: UniProtKB-EC
    2. carbohydrate binding Source: InterPro
    Complete GO annotation...

    GO - Biological processi

      Complete GO annotation...

      Keywords - Molecular functioni

      Glycosyltransferase, Transferase

      Keywords - Biological processi

      Carbohydrate metabolism

      Enzyme and pathway databases

      BRENDAi2.4.1.25. 6302.

      Protein family/group databases

      CAZyiGH57. Glycoside Hydrolase Family 57.

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      4-alpha-glucanotransferase (EC:2.4.1.25)
      Alternative name(s):
      Amylomaltase
      Disproportionating enzyme
      Short name:
      D-enzyme
      Gene namesi
      Name:jgt
      ORF Names:OCC_10078
      OrganismiThermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
      Taxonomic identifieri523849 [NCBI]
      Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
      ProteomesiUP000015502: Chromosome

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – 6596594-alpha-glucanotransferase
      PRO_0000184577Add
      BLAST

      Expressioni

      Inductioni

      Expressed constitutively.1 Publication

      Interactioni

      Subunit structurei

      homodimer.1 Publication

      Structurei

      Secondary structure

      Legend: HelixTurnBeta strand
      Show more details
      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Beta strandi4 – 129
      Helixi20 – 2910
      Helixi31 – 388
      Beta strandi46 – 505
      Helixi52 – 6110
      Helixi63 – 7412
      Beta strandi78 – 825
      Helixi90 – 923
      Helixi95 – 11117
      Beta strandi118 – 1203
      Helixi122 – 1243
      Helixi130 – 1367
      Beta strandi141 – 1455
      Helixi146 – 1527
      Helixi156 – 1583
      Beta strandi163 – 1675
      Beta strandi170 – 1778
      Helixi179 – 1846
      Turni185 – 1873
      Helixi190 – 1989
      Beta strandi208 – 2147
      Helixi215 – 2173
      Turni218 – 2203
      Helixi224 – 2285
      Turni229 – 2313
      Helixi233 – 24311
      Beta strandi247 – 2493
      Helixi252 – 2587
      Helixi274 – 2785
      Helixi282 – 29615
      Turni297 – 2993
      Turni302 – 3043
      Helixi305 – 3073
      Helixi313 – 3153
      Helixi316 – 3194
      Helixi321 – 33717
      Helixi341 – 35010
      Helixi353 – 3564
      Beta strandi359 – 3613
      Helixi363 – 3653
      Helixi367 – 38115
      Beta strandi389 – 3913
      Beta strandi393 – 3986
      Beta strandi400 – 4045
      Beta strandi406 – 4127
      Turni414 – 4185
      Beta strandi420 – 4256
      Turni426 – 4294
      Helixi442 – 4443
      Helixi472 – 4754
      Beta strandi487 – 4937
      Helixi499 – 5035
      Turni504 – 5063
      Beta strandi514 – 5163
      Beta strandi519 – 5235
      Beta strandi526 – 55227
      Beta strandi555 – 56612
      Beta strandi570 – 5789
      Beta strandi588 – 59912
      Turni600 – 6034
      Beta strandi604 – 62724
      Beta strandi630 – 65829

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      EntryMethodResolution (Å)ChainPositionsPDBsum
      1K1WX-ray2.80A1-659[»]
      1K1XX-ray2.40A/B1-659[»]
      1K1YX-ray2.40A/B1-659[»]
      ProteinModelPortaliO32462.
      SMRiO32462. Positions 2-659.

      Miscellaneous databases

      EvolutionaryTraceiO32462.

      Family & Domainsi

      Sequence similaritiesi

      Family and domain databases

      Gene3Di2.70.98.10. 1 hit.
      3.20.110.10. 2 hits.
      InterProiIPR015179. A-amylase/a-glucTrfase_C.
      IPR015178. A-amylase/a-glucTrfase_central.
      IPR011013. Gal_mutarotase_SF_dom.
      IPR014718. Glyco_hydro-type_carb-bd_sub.
      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]
      PfamiPF09094. DUF1925. 1 hit.
      PF09095. DUF1926. 1 hit.
      PF03065. Glyco_hydro_57. 1 hit.
      [Graphical view]
      ProDomiPD014405. DUF1925. 1 hit.
      [Graphical view] [Entries sharing at least one domain]
      SUPFAMiSSF74650. SSF74650. 1 hit.
      SSF88688. SSF88688. 1 hit.
      SSF88713. SSF88713. 1 hit.

      Sequencei

      Sequence statusi: Complete.

      O32462-1 [UniParc]FASTAAdd to Basket

      « Hide

      MERINFIFGI HNHQPLGNFG WVFEEAYNRS YRPFMEILEE FPEMKVNVHF    50
      SGPLLEWIEE NKPDYLDLLR SLIKRGQLEI VVAGFYEPVL AAIPKEDRLV 100
      QIEMLKDYAR KLGYDAKGVW LTERVWQPEL VKSLREAGIE YVVVDDYHFM 150
      SAGLSKEELF WPYYTEDGGE VITVFPIDEK LRYLIPFRPV KKTIEYLESL 200
      TSDDPSKVAV FHDDGEKFGV WPGTYEWVYE KGWLREFFDA ITSNEKINLM 250
      TYSEYLSKFT PRGLVYLPIA SYFEMSEWSL PAKQAKLFVE FVEQLKEEGK 300
      FEKYRVFVRG GIWKNFFFKY PESNFMHKRM LMVSKAVRDN PEARKYILKA 350
      QCNDAYWHGV FGGIYLPHLR RTVWENIIKA QRYLKPENKI LDVDFDGRAE 400
      IMVENDGFIA TIKPHYGGSI FELSSKRKAV NYNDVLPRRW EHYHEVPEAT 450
      KPEKESEEGI ASIHELGKQI PEEIRRELAY DWQLRAILQD HFIKPEETLD 500
      NYRLVKYHEL GDFVNQPYEY EMIENGVKLW REGGVYAEEK IPARVEKKIE 550
      LTEDGFIAKY RVLLEKPYKA LFGVEINLAV HSVMEKPEEF EAKEFEVNDP 600
      YGIGKVRIEL DKAAKVWKFP IKTLSQSEAG WDFIQQGVSY TMLFPIEKEL 650
      EFTVRFREL 659
      Length:659
      Mass (Da):77,885
      Last modified:January 1, 1998 - v1
      Checksum:iF789AFF9BF8281AC
      GO

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      D88253 Genomic DNA. Translation: BAA22063.1.
      CP006670 Genomic DNA. Translation: EHR79231.1.
      RefSeqiWP_004067291.1. NC_022084.1.
      YP_008428452.1. NC_022084.1.

      Genome annotation databases

      GeneIDi16548782.

      Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      D88253 Genomic DNA. Translation: BAA22063.1 .
      CP006670 Genomic DNA. Translation: EHR79231.1 .
      RefSeqi WP_004067291.1. NC_022084.1.
      YP_008428452.1. NC_022084.1.

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      Entry Method Resolution (Å) Chain Positions PDBsum
      1K1W X-ray 2.80 A 1-659 [» ]
      1K1X X-ray 2.40 A/B 1-659 [» ]
      1K1Y X-ray 2.40 A/B 1-659 [» ]
      ProteinModelPortali O32462.
      SMRi O32462. Positions 2-659.
      ModBasei Search...

      Protein family/group databases

      CAZyi GH57. Glycoside Hydrolase Family 57.

      Protocols and materials databases

      Structural Biology Knowledgebase Search...

      Genome annotation databases

      GeneIDi 16548782.

      Enzyme and pathway databases

      BRENDAi 2.4.1.25. 6302.

      Miscellaneous databases

      EvolutionaryTracei O32462.

      Family and domain databases

      Gene3Di 2.70.98.10. 1 hit.
      3.20.110.10. 2 hits.
      InterProi IPR015179. A-amylase/a-glucTrfase_C.
      IPR015178. A-amylase/a-glucTrfase_central.
      IPR011013. Gal_mutarotase_SF_dom.
      IPR014718. Glyco_hydro-type_carb-bd_sub.
      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 PF09094. DUF1925. 1 hit.
      PF09095. DUF1926. 1 hit.
      PF03065. Glyco_hydro_57. 1 hit.
      [Graphical view ]
      ProDomi PD014405. DUF1925. 1 hit.
      [Graphical view ] [Entries sharing at least one domain ]
      SUPFAMi SSF74650. SSF74650. 1 hit.
      SSF88688. SSF88688. 1 hit.
      SSF88713. SSF88713. 1 hit.
      ProtoNeti Search...

      Publicationsi

      « Hide 'large scale' publications
      1. "4-alpha-glucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis. Enzyme purification and characterization, and gene cloning, sequencing and expression in Escherichia coli."
        Jeon B.-S., Taguchi H., Sakai H., Ohshima T., Wakagi T., Matsuzawa H.
        Eur. J. Biochem. 248:171-178(1997) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19 AND 427-437, CHARACTERIZATION.
        Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
      2. "Genome sequence of the model hyperthermophilic archaeon Thermococcus litoralis NS-C."
        Gardner A.F., Kumar S., Perler F.B.
        J. Bacteriol. 194:2375-2376(2012) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
        Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
      3. "Maltose metabolism in the hyperthermophilic archaeon Thermococcus litoralis: purification and characterization of key enzymes."
        Xavier K.B., Peist R., Kossmann M., Boos W., Santos H.
        J. Bacteriol. 181:3358-3367(1999) [PubMed] [Europe PMC] [Abstract]
        Cited for: PROTEIN SEQUENCE OF 1-35, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION.
        Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
      4. "Crystal structures of 4-alpha-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor."
        Imamura H., Fushinobu S., Yamamoto M., Kumasaka T., Jeon B.S., Wakagi T., Matsuzawa H.
        J. Biol. Chem. 278:19378-19386(2003) [PubMed] [Europe PMC] [Abstract]
        Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

      Entry informationi

      Entry nameiMALQ_THELN
      AccessioniPrimary (citable) accession number: O32462
      Secondary accession number(s): H3ZLH6
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: August 29, 2001
      Last sequence update: January 1, 1998
      Last modified: September 3, 2014
      This is version 78 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, Direct protein sequencing

      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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