GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

CLOBU:MALQ

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Clostridium butyricum. (1492)
Gene Name(s) malQ
Protein Name(s) 4-alpha-glucanotransferase

Amylomaltase Disproportionating enzyme D-enzyme

External Links
UniProt Q59266
EMBL L37874
ProteinModelPortal Q59266
CAZy GH77
BRENDA 2.4.1.25
GO GO:0005737
GO:0004134
GO:0016757
Gene3D 3.20.20.80
InterPro IPR003385
IPR013781
IPR017853
Pfam PF02446
SUPFAM SSF51445
TIGRFAMs TIGR00217

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0016757

transferase activity, transferring glycosyl groups

PMID:9353929[1]

ECO:0000314

F

See figures 3 & 4

complete
CACAO 3291

GO:0004134

4-alpha-glucanotransferase activity

PMID:9353929[1]

ECO:0000314

F

See Figures 3 and 5.

Deletion subcloning of its recombinant plasmid indicated that the gene(s) responsible for amylose degradation was localized on a 1.8 kb NspHI-Scal fragment. This region was sequenced in its entirety and shown to encompass a large ORF capable of encoding a protein with a calculated molecular mass of 57,184 Da. Although the deduced amino acid sequence showed only weak similarity with known amylases, significant sequences identity was apparent with the 4-alpha-glucano-transferase enzymes of Streptococcus pneumoniae (46.9%), potato (42.9%) and E. coli (16.2%). The clostridial gene (designated maIQ) was followed by a second ORF which, through its homology to the equivalent enzymes of E. coli and S. pneumoniae, was deduced to encode maltodextrin phosphorylase (MaIP). The translation stop codon of MaIQ overlapped the translation start codon of the putative maIP gene, suggesting that the two genes may be both transcriptionally and translationally coupled. 4-alpha-Glucanotransferase catalyses a disproportionation reaction in which single or multiple glucose units from oligosaccharides are transferred to the 4-hydroxyl group of acceptor sugars. Characterization of the recombinant C. butyricum enzyme demonstrated that glucose, maltose and maltotriose could act as acceptor, whereas of the three only maltotriose could act as donor. The enzyme therefore shares properties with the E. coli MaIQ protein, but differs significantly from the glucanotransferase of Thermotoga maritima, which is unable to use maltotriose as donor or glucose as acceptor. Physiologically, the concerted action of 4-alpha-glucanotransferase and maltodextrin phosphorylase provides C. butyricum with a mechanism of utilizing amylose/maltodextrins with little drain on cellular ATP reserves

complete
CACAO 3325

enables

GO:0016757

transferase activity, transferring glycosyl groups

PMID:9353929[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0005977

glycogen metabolic process

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004134

P

Seeded From UniProt

complete

involved_in

GO:0005977

glycogen metabolic process

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004134

P

Seeded From UniProt

complete

enables

GO:0004134

4-alpha-glucanotransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003385

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003385

P

Seeded From UniProt

complete

enables

GO:0102500

beta-maltose 4-alpha-glucanotransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.4.1.25

F

Seeded From UniProt

complete

enables

GO:0004134

4-alpha-glucanotransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.4.1.25

F

Seeded From UniProt

complete

enables

GO:0016757

transferase activity, transferring glycosyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0328

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0119

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 Goda, SK et al. (1997) Molecular analysis of a Clostridium butyricum NCIMB 7423 gene encoding 4-alpha-glucanotransferase and characterization of the recombinant enzyme produced in Escherichia coli. Microbiology (Reading, Engl.) 143 ( Pt 10) 3287-94 PubMed GONUTS page