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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: 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

    1. Vmax=13 µmol/min/mg enzyme with maltose as substrate1 Publication
    2. 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)DescriptionActionsGraphical viewLength
    Active sitei123Nucleophile1
    Active sitei214Proton donor1

    GO - Molecular functioni

    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
    Proteomesi
    • UP000015502 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001845771 – 6594-alpha-glucanotransferaseAdd BLAST659

    Proteomic databases

    PRIDEiO32462.

    Expressioni

    Inductioni

    Expressed constitutively.1 Publication

    Interactioni

    Subunit structurei

    homodimer.1 Publication

    Structurei

    Secondary structure

    1659
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 12Combined sources9
    Helixi20 – 29Combined sources10
    Helixi31 – 38Combined sources8
    Beta strandi46 – 50Combined sources5
    Helixi52 – 61Combined sources10
    Helixi63 – 74Combined sources12
    Beta strandi78 – 82Combined sources5
    Helixi90 – 92Combined sources3
    Helixi95 – 111Combined sources17
    Beta strandi118 – 120Combined sources3
    Helixi122 – 124Combined sources3
    Helixi130 – 136Combined sources7
    Beta strandi141 – 145Combined sources5
    Helixi146 – 152Combined sources7
    Helixi156 – 158Combined sources3
    Beta strandi163 – 167Combined sources5
    Beta strandi170 – 177Combined sources8
    Helixi179 – 184Combined sources6
    Turni185 – 187Combined sources3
    Helixi190 – 198Combined sources9
    Beta strandi208 – 214Combined sources7
    Helixi215 – 217Combined sources3
    Turni218 – 220Combined sources3
    Helixi224 – 228Combined sources5
    Turni229 – 231Combined sources3
    Helixi233 – 243Combined sources11
    Beta strandi247 – 249Combined sources3
    Helixi252 – 258Combined sources7
    Helixi274 – 278Combined sources5
    Helixi282 – 296Combined sources15
    Turni297 – 299Combined sources3
    Turni302 – 304Combined sources3
    Helixi305 – 307Combined sources3
    Helixi313 – 315Combined sources3
    Helixi316 – 319Combined sources4
    Helixi321 – 337Combined sources17
    Helixi341 – 350Combined sources10
    Helixi353 – 356Combined sources4
    Beta strandi359 – 361Combined sources3
    Helixi363 – 365Combined sources3
    Helixi367 – 381Combined sources15
    Beta strandi389 – 391Combined sources3
    Beta strandi393 – 398Combined sources6
    Beta strandi400 – 404Combined sources5
    Beta strandi406 – 412Combined sources7
    Turni414 – 418Combined sources5
    Beta strandi420 – 425Combined sources6
    Turni426 – 429Combined sources4
    Helixi442 – 444Combined sources3
    Helixi472 – 475Combined sources4
    Beta strandi487 – 493Combined sources7
    Helixi499 – 503Combined sources5
    Turni504 – 506Combined sources3
    Beta strandi514 – 516Combined sources3
    Beta strandi519 – 523Combined sources5
    Beta strandi526 – 552Combined sources27
    Beta strandi555 – 566Combined sources12
    Beta strandi570 – 578Combined sources9
    Beta strandi588 – 599Combined sources12
    Turni600 – 603Combined sources4
    Beta strandi604 – 627Combined sources24
    Beta strandi630 – 658Combined sources29

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1K1WX-ray2.80A1-659[»]
    1K1XX-ray2.40A/B1-659[»]
    1K1YX-ray2.40A/B1-659[»]
    ProteinModelPortaliO32462.
    SMRiO32462.
    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. GH-type_carb-bd.
    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.

    Genome annotation databases

    EnsemblBacteriaiEHR79231; EHR79231; OCC_10078.
    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.
    RefSeqiWP_004067291.1. NC_022084.1.

    3D structure databases

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

    Protein family/group databases

    CAZyiGH57. Glycoside Hydrolase Family 57.

    Proteomic databases

    PRIDEiO32462.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiEHR79231; EHR79231; OCC_10078.
    GeneIDi16548782.
    KEGGitlt:OCC_10078.

    Enzyme and pathway databases

    BRENDAi2.4.1.25. 6302.

    Miscellaneous databases

    EvolutionaryTraceiO32462.
    PROiO32462.

    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. GH-type_carb-bd.
    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.
    ProtoNetiSearch...

    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 2, 2016
    This is version 94 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.