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O32462

- MALQ_THELN

UniProt

O32462 - MALQ_THELN

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Protein

4-alpha-glucanotransferase

Gene

jgt

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 substrate1 Publication

    Temperature dependencei

    Optimum temperature is 85-100 degrees Celsius.1 Publication

    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...

    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-glucanotransferasePRO_0000184577Add
    BLAST

    Expressioni

    Inductioni

    Expressed constitutively.1 Publication

    Interactioni

    Subunit structurei

    homodimer.1 Publication

    Structurei

    Secondary structure

    1
    659
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 129Combined sources
    Helixi20 – 2910Combined sources
    Helixi31 – 388Combined sources
    Beta strandi46 – 505Combined sources
    Helixi52 – 6110Combined sources
    Helixi63 – 7412Combined sources
    Beta strandi78 – 825Combined sources
    Helixi90 – 923Combined sources
    Helixi95 – 11117Combined sources
    Beta strandi118 – 1203Combined sources
    Helixi122 – 1243Combined sources
    Helixi130 – 1367Combined sources
    Beta strandi141 – 1455Combined sources
    Helixi146 – 1527Combined sources
    Helixi156 – 1583Combined sources
    Beta strandi163 – 1675Combined sources
    Beta strandi170 – 1778Combined sources
    Helixi179 – 1846Combined sources
    Turni185 – 1873Combined sources
    Helixi190 – 1989Combined sources
    Beta strandi208 – 2147Combined sources
    Helixi215 – 2173Combined sources
    Turni218 – 2203Combined sources
    Helixi224 – 2285Combined sources
    Turni229 – 2313Combined sources
    Helixi233 – 24311Combined sources
    Beta strandi247 – 2493Combined sources
    Helixi252 – 2587Combined sources
    Helixi274 – 2785Combined sources
    Helixi282 – 29615Combined sources
    Turni297 – 2993Combined sources
    Turni302 – 3043Combined sources
    Helixi305 – 3073Combined sources
    Helixi313 – 3153Combined sources
    Helixi316 – 3194Combined sources
    Helixi321 – 33717Combined sources
    Helixi341 – 35010Combined sources
    Helixi353 – 3564Combined sources
    Beta strandi359 – 3613Combined sources
    Helixi363 – 3653Combined sources
    Helixi367 – 38115Combined sources
    Beta strandi389 – 3913Combined sources
    Beta strandi393 – 3986Combined sources
    Beta strandi400 – 4045Combined sources
    Beta strandi406 – 4127Combined sources
    Turni414 – 4185Combined sources
    Beta strandi420 – 4256Combined sources
    Turni426 – 4294Combined sources
    Helixi442 – 4443Combined sources
    Helixi472 – 4754Combined sources
    Beta strandi487 – 4937Combined sources
    Helixi499 – 5035Combined sources
    Turni504 – 5063Combined sources
    Beta strandi514 – 5163Combined sources
    Beta strandi519 – 5235Combined sources
    Beta strandi526 – 55227Combined sources
    Beta strandi555 – 56612Combined sources
    Beta strandi570 – 5789Combined sources
    Beta strandi588 – 59912Combined sources
    Turni600 – 6034Combined sources
    Beta strandi604 – 62724Combined sources
    Beta strandi630 – 65829Combined sources

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiO32462.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 57 family.Curated

    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

            10         20         30         40         50
    MERINFIFGI HNHQPLGNFG WVFEEAYNRS YRPFMEILEE FPEMKVNVHF
    60 70 80 90 100
    SGPLLEWIEE NKPDYLDLLR SLIKRGQLEI VVAGFYEPVL AAIPKEDRLV
    110 120 130 140 150
    QIEMLKDYAR KLGYDAKGVW LTERVWQPEL VKSLREAGIE YVVVDDYHFM
    160 170 180 190 200
    SAGLSKEELF WPYYTEDGGE VITVFPIDEK LRYLIPFRPV KKTIEYLESL
    210 220 230 240 250
    TSDDPSKVAV FHDDGEKFGV WPGTYEWVYE KGWLREFFDA ITSNEKINLM
    260 270 280 290 300
    TYSEYLSKFT PRGLVYLPIA SYFEMSEWSL PAKQAKLFVE FVEQLKEEGK
    310 320 330 340 350
    FEKYRVFVRG GIWKNFFFKY PESNFMHKRM LMVSKAVRDN PEARKYILKA
    360 370 380 390 400
    QCNDAYWHGV FGGIYLPHLR RTVWENIIKA QRYLKPENKI LDVDFDGRAE
    410 420 430 440 450
    IMVENDGFIA TIKPHYGGSI FELSSKRKAV NYNDVLPRRW EHYHEVPEAT
    460 470 480 490 500
    KPEKESEEGI ASIHELGKQI PEEIRRELAY DWQLRAILQD HFIKPEETLD
    510 520 530 540 550
    NYRLVKYHEL GDFVNQPYEY EMIENGVKLW REGGVYAEEK IPARVEKKIE
    560 570 580 590 600
    LTEDGFIAKY RVLLEKPYKA LFGVEINLAV HSVMEKPEEF EAKEFEVNDP
    610 620 630 640 650
    YGIGKVRIEL DKAAKVWKFP IKTLSQSEAG WDFIQQGVSY TMLFPIEKEL

    EFTVRFREL
    Length:659
    Mass (Da):77,885
    Last modified:January 1, 1998 - v1
    Checksum:iF789AFF9BF8281AC
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.
    KEGGitlt:OCC_10078.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    PDBei
    RCSB PDBi
    PDBji
    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...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH57. Glycoside Hydrolase Family 57.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 16548782.
    KEGGi tlt:OCC_10078.

    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: November 26, 2014
    This is version 81 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, 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