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B3PEE6

- OL4AG_CELJU

UniProt

B3PEE6 - OL4AG_CELJU

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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: 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. alpha-1,4-glucosidase activity Source: UniProtKB-EC
  2. carbohydrate binding Source: InterPro
  3. maltose alpha-glucosidase activity Source: UniProtKB-EC

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

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.
KOiK01187.
OMAiATWFDYY.
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 .
RefSeqi WP_012488824.1. NC_010995.1.
YP_001983702.1. NC_010995.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4B9Y X-ray 1.90 A 1-816 [» ]
4B9Z X-ray 2.00 A 1-816 [» ]
4BA0 X-ray 1.85 A 1-816 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 498211.CJA_3248.

Protein family/group databases

CAZyi GH31. Glycoside Hydrolase Family 31.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACE84782 ; ACE84782 ; CJA_3248 .
GeneIDi 6415228.
KEGGi cja:CJA_3248.
PATRICi 21329891. VBICelJap122165_3210.

Phylogenomic databases

eggNOGi COG1501.
HOGENOMi HOG000066231.
KOi K01187.
OMAi ATWFDYY.
OrthoDBi EOG67X1Q7.

Enzyme and pathway databases

BioCyci CJAP498211:GHIT-3237-MONOMER.

Family and domain databases

InterProi IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 43 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