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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Binding sitei299Alpha-acarbose1 Publication1
    Active sitei412Nucleophile1 Publication1
    Active sitei415By similarity1
    Binding sitei417Alpha-acarbose1 Publication1
    Binding sitei463Alpha-acarbose1 Publication1
    Active sitei480Proton donorBy similarity1
    Binding sitei480Alpha-acarbose1 Publication1
    Binding sitei540Alpha-acarbose1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeCellvibrio
    Proteomesi
    • UP000001036 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 24Sequence analysisAdd BLAST24
    ChainiPRO_000043070025 – 816Oligosaccharide 4-alpha-D-glucosyltransferaseSequence analysisAdd BLAST792

    Interactioni

    Protein-protein interaction databases

    STRINGi498211.CJA_3248.

    Structurei

    Secondary structure

    1816
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi38 – 42Combined sources5
    Beta strandi45 – 52Combined sources8
    Beta strandi55 – 63Combined sources9
    Beta strandi66 – 72Combined sources7
    Beta strandi93 – 96Combined sources4
    Beta strandi98 – 104Combined sources7
    Beta strandi106 – 113Combined sources8
    Turni114 – 117Combined sources4
    Beta strandi118 – 123Combined sources6
    Beta strandi126 – 136Combined sources11
    Beta strandi142 – 147Combined sources6
    Beta strandi154 – 159Combined sources6
    Beta strandi169 – 173Combined sources5
    Beta strandi185 – 187Combined sources3
    Beta strandi191 – 197Combined sources7
    Beta strandi200 – 205Combined sources6
    Beta strandi209 – 219Combined sources11
    Beta strandi222 – 230Combined sources9
    Beta strandi233 – 238Combined sources6
    Helixi242 – 253Combined sources12
    Helixi261 – 264Combined sources4
    Beta strandi265 – 268Combined sources4
    Helixi276 – 289Combined sources14
    Beta strandi295 – 298Combined sources4
    Helixi300 – 302Combined sources3
    Beta strandi305 – 309Combined sources5
    Turni318 – 320Combined sources3
    Helixi324 – 333Combined sources10
    Beta strandi337 – 342Combined sources6
    Beta strandi344 – 347Combined sources4
    Helixi353 – 358Combined sources6
    Beta strandi368 – 370Combined sources3
    Beta strandi373 – 375Combined sources3
    Beta strandi378 – 383Combined sources6
    Helixi388 – 404Combined sources17
    Beta strandi408 – 411Combined sources4
    Turni414 – 416Combined sources3
    Helixi430 – 433Combined sources4
    Helixi434 – 436Combined sources3
    Helixi437 – 452Combined sources16
    Beta strandi460 – 463Combined sources4
    Helixi469 – 472Combined sources4
    Beta strandi474 – 477Combined sources4
    Beta strandi482 – 484Combined sources3
    Helixi485 – 489Combined sources5
    Helixi491 – 500Combined sources10
    Helixi521 – 532Combined sources12
    Helixi549 – 551Combined sources3
    Helixi554 – 569Combined sources16
    Helixi571 – 584Combined sources14
    Beta strandi588 – 591Combined sources4
    Helixi592 – 595Combined sources4
    Helixi600 – 604Combined sources5
    Beta strandi609 – 611Combined sources3
    Turni612 – 614Combined sources3
    Beta strandi615 – 617Combined sources3
    Beta strandi627 – 630Combined sources4
    Beta strandi634 – 639Combined sources6
    Turni640 – 642Combined sources3
    Beta strandi645 – 651Combined sources7
    Beta strandi653 – 656Combined sources4
    Beta strandi664 – 667Combined sources4
    Beta strandi671 – 674Combined sources4
    Helixi681 – 683Combined sources3
    Beta strandi687 – 694Combined sources8
    Beta strandi700 – 708Combined sources9
    Turni714 – 720Combined sources7
    Beta strandi722 – 731Combined sources10
    Beta strandi733 – 744Combined sources12
    Beta strandi752 – 761Combined sources10
    Beta strandi769 – 772Combined sources4
    Beta strandi775 – 778Combined sources4
    Helixi784 – 786Combined sources3
    Beta strandi790 – 794Combined sources5
    Turni795 – 798Combined sources4
    Beta strandi799 – 806Combined sources8
    Beta strandi811 – 816Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4B9YX-ray1.90A1-816[»]
    4B9ZX-ray2.00A1-816[»]
    4BA0X-ray1.85A1-816[»]
    5I23X-ray1.95A25-816[»]
    5I24X-ray1.85A25-816[»]
    SMRiB3PEE6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105CJQ. Bacteria.
    COG1501. LUCA.
    HOGENOMiHOG000066231.
    KOiK18820.
    OMAiGVAGWWG.
    OrthoDBiPOG091H06L9.

    Family and domain databases

    InterProiIPR032513. DUF4968.
    IPR033403. DUF5110.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF16338. DUF4968. 1 hit.
    PF17137. DUF5110. 1 hit.
    PF13802. 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.
    RefSeqiWP_012488824.1. NC_010995.1.

    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.
    RefSeqiWP_012488824.1. NC_010995.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4B9YX-ray1.90A1-816[»]
    4B9ZX-ray2.00A1-816[»]
    4BA0X-ray1.85A1-816[»]
    5I23X-ray1.95A25-816[»]
    5I24X-ray1.85A25-816[»]
    SMRiB3PEE6.
    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

    eggNOGiENOG4105CJQ. Bacteria.
    COG1501. LUCA.
    HOGENOMiHOG000066231.
    KOiK18820.
    OMAiGVAGWWG.
    OrthoDBiPOG091H06L9.

    Family and domain databases

    InterProiIPR032513. DUF4968.
    IPR033403. DUF5110.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF16338. DUF4968. 1 hit.
    PF17137. DUF5110. 1 hit.
    PF13802. Gal_mutarotas_2. 1 hit.
    PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF74650. SSF74650. 1 hit.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 52 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

    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.