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O87172

- MALQ_THETH

UniProt

O87172 - MALQ_THETH

Protein

4-alpha-glucanotransferase

Gene

malQ

Organism
Thermus thermophilus
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. 4-alpha-glucanotransferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Protein family/group databases

    CAZyiGH77. Glycoside Hydrolase Family 77.

    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:malQ
    OrganismiThermus thermophilus
    Taxonomic identifieri274 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5005004-alpha-glucanotransferasePRO_0000170132Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi262724.TTC0897.

    Structurei

    Secondary structure

    1
    500
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Helixi13 – 153
    Beta strandi19 – 224
    Helixi27 – 3812
    Beta strandi43 – 453
    Beta strandi60 – 623
    Helixi69 – 713
    Helixi75 – 795
    Beta strandi92 – 943
    Helixi97 – 11822
    Helixi121 – 15030
    Turni151 – 1533
    Helixi156 – 1583
    Helixi161 – 1644
    Helixi168 – 17710
    Helixi179 – 20527
    Beta strandi209 – 2179
    Beta strandi220 – 2223
    Helixi223 – 2275
    Helixi229 – 2313
    Beta strandi240 – 2434
    Beta strandi256 – 2616
    Helixi265 – 2706
    Turni271 – 2733
    Helixi274 – 28613
    Beta strandi288 – 2936
    Helixi295 – 2984
    Beta strandi300 – 3056
    Beta strandi309 – 3113
    Beta strandi315 – 3184
    Helixi321 – 33212
    Beta strandi337 – 3393
    Helixi347 – 3559
    Beta strandi360 – 3634
    Helixi364 – 3663
    Beta strandi367 – 3704
    Helixi378 – 3803
    Beta strandi387 – 3915
    Helixi399 – 4057
    Helixi408 – 42013
    Helixi428 – 4303
    Helixi431 – 44111
    Beta strandi445 – 4506
    Helixi451 – 4544
    Helixi459 – 4613
    Beta strandi469 – 4713
    Turni479 – 4813
    Helixi484 – 49613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CWYX-ray2.00A1-500[»]
    1ESWX-ray1.90A1-500[»]
    1FP8X-ray2.30A1-500[»]
    1FP9X-ray3.10A1-500[»]
    2OWCX-ray2.05A1-500[»]
    2OWWX-ray2.20A1-500[»]
    2OWXX-ray2.50A1-500[»]
    ProteinModelPortaliO87172.
    SMRiO87172. Positions 1-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO87172.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the disproportionating enzyme family.Curated

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR003385. Glyco_hydro_77.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF02446. Glyco_hydro_77. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    TIGRFAMsiTIGR00217. malQ. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O87172-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELPRAFGLL LHPTSLPGPY GVGVLGREAR DFLRFLKEAG GRYWQVLPLG    50
    PTGYGDSPYQ SFSAFAGNPY LIDLRPLAER GYVRLEDPGF PQGRVDYGLL 100
    YAWKWPALKE AFRGFKEKAS PEEREAFAAF REREAWWLED YALFMALKGA 150
    HGGLPWNRWP LPLRKREEKA LREAKSALAE EVAFHAFTQW LFFRQWGALK 200
    AEAEALGIRI IGDMPIFVAE DSAEVWAHPE WFHLDEEGRP TVVAGVPPDY 250
    FSETGQRWGN PLYRWDVLER EGFSFWIRRL EKALELFHLV RIDHFRGFEA 300
    YWEIPASCPT AVEGRWVKAP GEKLFQKIQE VFGEVPVLAE DLGVITPEVE 350
    ALRDRFGLPG MKVLQFAFDD GMENPFLPHN YPAHGRVVVY TGTHDNDTTL 400
    GWYRTATPHE KAFMARYLAD WGITFREEEE VPWALMHLGM KSVARLAVYP 450
    VQDVLALGSE ARMNYPGRPS GNWAWRLLPG ELSPEHGARL RAMAEATERL 500
    Length:500
    Mass (Da):57,222
    Last modified:November 1, 1998 - v1
    Checksum:i6E7175A38E0A5D61
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB016244 Genomic DNA. Translation: BAA33728.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB016244 Genomic DNA. Translation: BAA33728.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CWY X-ray 2.00 A 1-500 [» ]
    1ESW X-ray 1.90 A 1-500 [» ]
    1FP8 X-ray 2.30 A 1-500 [» ]
    1FP9 X-ray 3.10 A 1-500 [» ]
    2OWC X-ray 2.05 A 1-500 [» ]
    2OWW X-ray 2.20 A 1-500 [» ]
    2OWX X-ray 2.50 A 1-500 [» ]
    ProteinModelPortali O87172.
    SMRi O87172. Positions 1-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 262724.TTC0897.

    Protein family/group databases

    CAZyi GH77. Glycoside Hydrolase Family 77.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei O87172.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR003385. Glyco_hydro_77.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF02446. Glyco_hydro_77. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    TIGRFAMsi TIGR00217. malQ. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression and characterization of amylomaltase from Thermus aquaticus ATCC33923."
      Terada Y., Fujii K., Takaha T., Okada S.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 33923 / DSM 674 / AT-62.
    2. "Crystal structure of amylomaltase from Thermus aquaticus, a glycosyltransferase catalysing the production of large cyclic glucans."
      Przylas I., Tomoo K., Terada Y., Takaha T., Fujii K., Saenger W., Strater N.
      J. Mol. Biol. 296:873-886(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiMALQ_THETH
    AccessioniPrimary (citable) accession number: O87172
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1998
    Last modified: October 1, 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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3