CLOBU:MALQ

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	ECO:0000314			F		See figures 3 & 4	complete CACAO 3291
	GO:0004134	4-alpha-glucanotransferase activity	PMID:9353929	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	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
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