CAZyme Information: MGYG000001937_01687

Basic Information

• Species: UBA7173 sp001701135
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp001701135
• CAZyme ID: MGYG000001937_01687
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
920		101453.22	6.1824

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001937	2244087	MAG	Denmark	Europe

• Gene Location: Start: 4511; End: 7273 Strand: +

Full Sequence      

MKKHYLLLLSMLLLAVASVQAAMFSTSPNPLQQSSKDVKIYFDPAQCDVAALKTASEIYA
HIGVTLPSAPSSWVYVVGDWADKQAKKKFVKQSDGRWMLNIGEIDTYFNLPAGTKVAKIA
IIALNAAGSSQTGDVYLDVAEEGYAMSLTSNPEDLVISKATNFTFTVGVTQPSTITIKVG
DQVIGTASNATTLTKSHNFATQGTFNEVTATATNGKETLTKSLTVAYPSASTAMNYPGGV
PKQGAIRQADGSVLFCIAAPSKTSAILVGSWDDFKTLNKNVMKYQDYNGYRYFWTRVEGL
ADRQYHSYYYLLDGVTKVADPYAKLILDPYSDKWLPSGIWNEPMPQYPYEKIDGVMLAVY
RSDLDDYKWDSATTNFKVPDHNSMVIYELLFRDFTGDGSDQDGKHFGTISEAREKISYLK
ELGINCVELMPVMEFNGNNSWGYNTNAYMALDKAYGSPKDLRDFVAECHRNGIAVVLDIV
FNQTDGLHPWYQMYPIASNPFYNEKAPHAYNVLNDVRQDYPLVEQHWADVLRYWMEAYKV
DGFRFDLVKGLGDNSSYTGGSTDSRNQSRINRMKRLNDVITSVKADGIHINELLGQNTEE
NDNFKNGAQMGWQNLNYTSYQNAMGFAAGSADVKNFNPGNGGRTFGAAVGYAESHDEVRI
AYKMKTGGANANIKYSGAHPGVTGVQRLGSVAAYMLMAPGAKMIWQFGEIGADDKLGSDL
EKLRAIAPKWDQFENENRKALFENYQALCYLRLKNPELFDGSADYVTSSFSNSLTSVRWI
KVRKGEKEVVAVINPQITGKTTQRINGIQKLNANNYHVVTKGYKSEPTVTFSGGAVSVQI
PSNSFIVIATNSVASTEEVSADMTAPAVNVYGSNGEIVIEGDYETAEVYDLQGRMSKSLQ
VPAGVYVVRVDGNAYKVAVK

Enzyme Prediction     

No EC number prediction in MGYG000001937_01687.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	402	714	5.6e-46	0.9565217391304348

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	1.15e-117	367	759	1	387	Alpha amylase catalytic domain found in an uncharacterized protein family. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
COG0296	GlgB	1.63e-46	244	867	27	620	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11325	AmyAc_GTHase	2.51e-40	363	555	19	197	Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase). Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase
COG1523	PulA	4.75e-39	308	547	84	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11326	AmyAc_Glg_debranch	1.86e-36	384	547	16	205	Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCD35300.1	1.03e-228	1	920	1	927
QIM10833.1	1.76e-209	22	920	8	908
QQR08212.1	2.01e-164	21	797	26	732
ANU64421.1	2.01e-164	21	797	26	732
ASB37479.1	2.01e-164	21	797	26	732

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4J7R_A	1.12e-23	324	551	157	422	CrystalStructure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) [Chlamydomonas reinhardtii],4J7R_B Crystal Structure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) [Chlamydomonas reinhardtii],4OKD_A Crystal Structure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) in complex with maltoheptaose [Chlamydomonas reinhardtii],4OKD_B Crystal Structure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) in complex with maltoheptaose [Chlamydomonas reinhardtii]
1EH9_A	4.51e-23	302	555	36	261	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	4.51e-23	302	555	36	261	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
1EHA_A	4.51e-23	302	555	36	261	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	1.40e-22	302	555	36	261	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P95867	8.49e-25	312	555	48	264	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
B9G434	6.08e-24	313	551	195	450	Isoamylase 3, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA3 PE=2 SV=1
O22637	2.46e-23	296	551	158	422	Isoamylase SU1, chloroplastic OS=Zea mays OX=4577 GN=SU1 PE=1 SV=1
B4TY88	9.41e-23	323	762	89	568	Glycogen debranching enzyme OS=Salmonella schwarzengrund (strain CVM19633) OX=439843 GN=glgX PE=3 SV=1
B5F8Q3	9.41e-23	323	762	89	568	Glycogen debranching enzyme OS=Salmonella agona (strain SL483) OX=454166 GN=glgX PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000290	0.998990	0.000198	0.000167	0.000170	0.000159

TMHMM  Annotations     

start	end
5	24