Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

  1. carbohydrate binding Source: InterPro
  2. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro
  3. oligosaccharide 4-alpha-D-glucosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
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: 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.
OMAiGLQRYAW.
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.
RefSeqiWP_012488824.1. NC_010995.1.
YP_001983702.1. NC_010995.1.

Genome annotation databases

EnsemblBacteriaiACE84782; ACE84782; CJA_3248.
GeneIDi6415228.
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.
YP_001983702.1. NC_010995.1.

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.
GeneIDi6415228.
KEGGicja:CJA_3248.
PATRICi21329891. VBICelJap122165_3210.

Phylogenomic databases

eggNOGiCOG1501.
HOGENOMiHOG000066231.
KOiK18820.
OMAiGLQRYAW.
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: March 4, 2015
This is version 45 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.