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Protein

Oligosaccharide 4-alpha-D-glucosyltransferase

Gene

agd31B

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Alpha-transglucosylase that specifically transfers single glucosyl units from alpha(1->4)-glucans to the non-reducing terminal 4-OH of glucose and alpha(1->4)- and alpha(1->6)-linked glucosyl residues. Acts on amylose, amylopectin, glycogen and maltooligosaccharides, with the highest activity with maltotriose as a donor, and also accepts maltose. Does not act as a hydrolase: weak hydrolysis activity is only observed on the disaccharide maltose.1 Publication

Catalytic activityi

Transfers the non-reducing terminal alpha-D-glucose residue from a (1->4)-alpha-D-glucan to the 4-position of a free glucose or of a glucosyl residue at the non-reducing terminus of a (1->4)-alpha-D-glucan, thus bringing about the rearrangement of oligosaccharides.1 Publication

Kineticsi

kcat is 341 sec(-1) for maltose. kcat is 239 sec(-1) for maltotriose. kcat is 123 sec(-1) for maltotetraose. kcat is 181 sec(-1) for maltopentaose.1 Publication

  1. KM=8.8 mM for maltose1 Publication
  2. KM=1.2 mM for maltotriose1 Publication
  3. KM=1.7 mM for maltotetraose1 Publication
  4. KM=3.1 mM for maltopentaose1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei299 – 2991Alpha-acarbose1 Publication
    Active sitei412 – 4121Nucleophile1 Publication
    Active sitei415 – 4151By similarity
    Binding sitei417 – 4171Alpha-acarbose1 Publication
    Binding sitei463 – 4631Alpha-acarbose1 Publication
    Active sitei480 – 4801Proton donorBy similarity
    Binding sitei480 – 4801Alpha-acarbose1 Publication
    Binding sitei540 – 5401Alpha-acarbose1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciCJAP498211:GHIT-3237-MONOMER.

    Protein family/group databases

    CAZyiGH31. Glycoside Hydrolase Family 31.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oligosaccharide 4-alpha-D-glucosyltransferaseCurated (EC:2.4.1.1611 Publication)
    Alternative name(s):
    Alpha-glucosidase 31BCurated
    Short name:
    CJAgd31B1 Publication
    Gene namesi
    Name:agd31B1 Publication
    Ordered Locus Names:CJA_3248Imported
    OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)Imported
    Taxonomic identifieri498211 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio
    ProteomesiUP000001036 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 816792Oligosaccharide 4-alpha-D-glucosyltransferaseSequence AnalysisPRO_0000430700Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi498211.CJA_3248.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 425Combined sources
    Beta strandi45 – 528Combined sources
    Beta strandi55 – 639Combined sources
    Beta strandi66 – 727Combined sources
    Beta strandi93 – 964Combined sources
    Beta strandi98 – 1047Combined sources
    Beta strandi106 – 1138Combined sources
    Turni114 – 1174Combined sources
    Beta strandi118 – 1236Combined sources
    Beta strandi126 – 13611Combined sources
    Beta strandi142 – 1476Combined sources
    Beta strandi154 – 1596Combined sources
    Beta strandi169 – 1735Combined sources
    Beta strandi185 – 1873Combined sources
    Beta strandi191 – 1977Combined sources
    Beta strandi200 – 2056Combined sources
    Beta strandi209 – 21911Combined sources
    Beta strandi222 – 2309Combined sources
    Beta strandi233 – 2386Combined sources
    Helixi242 – 25312Combined sources
    Helixi261 – 2644Combined sources
    Beta strandi265 – 2684Combined sources
    Helixi276 – 28914Combined sources
    Beta strandi295 – 2984Combined sources
    Helixi300 – 3023Combined sources
    Beta strandi305 – 3095Combined sources
    Turni318 – 3203Combined sources
    Helixi324 – 33310Combined sources
    Beta strandi337 – 3426Combined sources
    Beta strandi344 – 3474Combined sources
    Helixi353 – 3586Combined sources
    Beta strandi368 – 3703Combined sources
    Beta strandi373 – 3753Combined sources
    Beta strandi378 – 3836Combined sources
    Helixi388 – 40417Combined sources
    Beta strandi408 – 4114Combined sources
    Turni414 – 4163Combined sources
    Helixi430 – 4334Combined sources
    Helixi434 – 4363Combined sources
    Helixi437 – 45216Combined sources
    Beta strandi460 – 4634Combined sources
    Helixi469 – 4724Combined sources
    Beta strandi474 – 4774Combined sources
    Beta strandi482 – 4843Combined sources
    Helixi485 – 4895Combined sources
    Helixi491 – 50010Combined sources
    Helixi521 – 53212Combined sources
    Helixi549 – 5513Combined sources
    Helixi554 – 56916Combined sources
    Helixi571 – 58414Combined sources
    Beta strandi588 – 5914Combined sources
    Helixi592 – 5954Combined sources
    Helixi600 – 6045Combined sources
    Beta strandi609 – 6113Combined sources
    Turni612 – 6143Combined sources
    Beta strandi615 – 6173Combined sources
    Beta strandi627 – 6304Combined sources
    Beta strandi634 – 6396Combined sources
    Turni640 – 6423Combined sources
    Beta strandi645 – 6517Combined sources
    Beta strandi653 – 6564Combined sources
    Beta strandi664 – 6674Combined sources
    Beta strandi671 – 6744Combined sources
    Helixi681 – 6833Combined sources
    Beta strandi687 – 6948Combined sources
    Beta strandi700 – 7089Combined sources
    Turni714 – 7207Combined sources
    Beta strandi722 – 73110Combined sources
    Beta strandi733 – 74412Combined sources
    Beta strandi752 – 76110Combined sources
    Beta strandi769 – 7724Combined sources
    Beta strandi775 – 7784Combined sources
    Helixi784 – 7863Combined sources
    Beta strandi790 – 7945Combined sources
    Turni795 – 7984Combined sources
    Beta strandi799 – 8068Combined sources
    Beta strandi811 – 8166Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4B9YX-ray1.90A1-816[»]
    4B9ZX-ray2.00A1-816[»]
    4BA0X-ray1.85A1-816[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1501.
    HOGENOMiHOG000066231.
    KOiK18820.
    OMAiNNISAHV.
    OrthoDBiEOG67X1Q7.

    Family and domain databases

    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF13802. Gal_mutarotas_2. 1 hit.
    PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF74650. SSF74650. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    B3PEE6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MFRRIAGFSP IFLMLFGSSL PTMGNPVKRE IHPDAVFYKE HKLRNDGLVI
    60 70 80 90 100
    TTNQGNIRLQ FKSEAAIEVL YRADSKQLPS FALAQPESAI KAQLTETENH
    110 120 130 140 150
    LQFSGGTLTA RIQKRPFAIS YYRDSELLLA EESGFQVNTD KINFRFYLSP
    160 170 180 190 200
    GEKILGGGQR ILGMDRRGQR FPLYNRAHYG YSDHSGQMYF GLPAIMSSKQ
    210 220 230 240 250
    YILVFDNSAS GAMDIGKTES DILQLEAKSG RSAYILVAGN SYPSLIENFT
    260 270 280 290 300
    QVTGRQPLPP RWALGSFASR FGYRSEAETR ATVQKYKTED FPLDTIVLDL
    310 320 330 340 350
    YWFGKDIKGH MGNLDWDKEN FPTPLDMMAD FKQQGVKTVL ITEPFVLTSS
    360 370 380 390 400
    KRWDDAVKAK ALAKDPQGQP KAFELYFGNG GIIDVFSKEG SRWFSSIYKD
    410 420 430 440 450
    LSKQGVAGWW GDLGEPEMHP EDTQHAIGDA DTVHNAYGHR WAEMLYQQQL
    460 470 480 490 500
    DQFPELRPFI MMRAGFVGSQ RYGMIPWTGD VSRTWGGLAS QVELALQMSL
    510 520 530 540 550
    LGFGYIHSDL GGFADGETLD KEMYIRWLQY GVFQPVYRPH GQDHIPSEPV
    560 570 580 590 600
    FQDEETKAIL RPLVKLRYRM LPYIYTAAYQ NTLTGMPLMR PLFFSDEKNP
    610 620 630 640 650
    ALIDNKTSYF WGDSLLVTPI TQAGVESVSI PAPKGVWFDF WKDTRYQTDG
    660 670 680 690 700
    APLTLPTDLH TIPVLVKAGA FMPYVPAVST TEDYRSDSLE IHYYADASVP
    710 720 730 740 750
    LAQGEIFEDD GKDPNSIKRN QFDLLTLQAT HTDNQLHFQL ARTGKGYRGM
    760 770 780 790 800
    PERRATTLVI HNASDQYQHL DINGKTIAIA QADCASTPAL ACYDQERRQL
    810
    QLVFTWGREA LNLRLH
    Length:816
    Mass (Da):92,279
    Last modified:September 2, 2008 - v1
    Checksum:i46C43AEBC564851B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000934 Genomic DNA. Translation: ACE84782.1.

    Genome annotation databases

    EnsemblBacteriaiACE84782; ACE84782; CJA_3248.
    KEGGicja:CJA_3248.
    PATRICi21329891. VBICelJap122165_3210.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000934 Genomic DNA. Translation: ACE84782.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4B9YX-ray1.90A1-816[»]
    4B9ZX-ray2.00A1-816[»]
    4BA0X-ray1.85A1-816[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi498211.CJA_3248.

    Protein family/group databases

    CAZyiGH31. Glycoside Hydrolase Family 31.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiACE84782; ACE84782; CJA_3248.
    KEGGicja:CJA_3248.
    PATRICi21329891. VBICelJap122165_3210.

    Phylogenomic databases

    eggNOGiCOG1501.
    HOGENOMiHOG000066231.
    KOiK18820.
    OMAiNNISAHV.
    OrthoDBiEOG67X1Q7.

    Enzyme and pathway databases

    BioCyciCJAP498211:GHIT-3237-MONOMER.

    Family and domain databases

    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF13802. Gal_mutarotas_2. 1 hit.
    PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF74650. SSF74650. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
      DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
      J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ueda107Imported.
    2. "Structural enzymology of Cellvibrio japonicus Agd31B protein reveals alpha-transglucosylase activity in glycoside hydrolase family 31."
      Larsbrink J., Izumi A., Hemsworth G.R., Davies G.J., Brumer H.
      J. Biol. Chem. 287:43288-43299(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH ALPHA-ACARBOSE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiOL4AG_CELJU
    AccessioniPrimary (citable) accession number: B3PEE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: September 2, 2008
    Last modified: July 22, 2015
    This is version 47 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

    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 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.