CAZyme Information: MGYG000000673_01754

Basic Information

• Species: CAG-873 sp004552485
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp004552485
• CAZyme ID: MGYG000000673_01754
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
918		100515.71	6.1485

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000673	2306526	MAG	Kazakhstan	Asia

• Gene Location: Start: 6547; End: 9303 Strand: +

Full Sequence      

MKKILTLLLAVMALTLSSAAQIVTTSPAILQESSKNVVLTYHADSPLGNNGLKGNTASDP
VYAHIGCVTNKSNGGWVYAPTWKDNSAKYKLNYVAANTWTLNLGDMRTYFGIKDASEHIE
KLAIVFRNGTASKEGKTKEGGDIFVEVVPEGFQMIFSTNATSTILNSAATLSFTAVTSQA
ANISITVDGKSIASASGKTELTASHKFSTHGSFDVVATATANGQTLTRSLNVAYPGQSTA
GTYPGGVPKMGAVKNADGSVTFCLAAPGKQSVVLVPSWDDYKVLDKNIMKYQDYNGQRYF
FSTVSGLDNNTDYPYYFLVDAKYKVGDPYAHLVLDNYSDRYLDKSIWPDMPQYPYDKFDD
VCLAVYNGSADFDFHFSDFKIPDHKNLVIYEMLFRDFTGTEGAANGEGTIRKAIEKFDHI
KSLGVNAVELMPVMEFNGNNSWGYNTNFYFALDKAYGSPRDLKEFVELCHQNGIAVILDI
VFNQSDGLHPWYRMYDISSNPFYNQTAPHSYSVLNDWKQENTLVRQQWKDCIKHWMTVYN
VDGFRFDLVKGLGTSYGSNTDAYNSSRVAVMKDLHSAIKAVKADGIHINENLAGNQEENE
MAADGQLNWANINNHACQYAMGYAADSRLNRFYSADDSRTDCSTVAYAESHDEERMGFKQ
NEYAPATVKGKTEISMWRLGSVAVQMLMVPGPKMIWQFGELGADQTTKDSGGGNDTSPKK
VIWSYKDNVDRKALFDTYRAMGCLRRDNPEMFNGTAGYTQTNLNQNNISSARTIRLVNGN
KEIIAFINPNTTTSRHLTVSSASSALKKANSQLIIASKNFNPTLTDTDSGVSCRVPGNGY
AVYATTNIAGVDDIIVDGGANGEASAVAIGGTGEIIIIGDYENVAVYNMSGALMPSLRVN
AGLYIVNIDGVASKVLVR

Enzyme Prediction     

No EC number prediction in MGYG000000673_01754.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	404	708	2.6e-44	0.9531772575250836

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	6.64e-127	372	755	1	390	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.
cd11325	AmyAc_GTHase	5.73e-47	369	653	20	318	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
COG0296	GlgB	3.82e-37	249	549	25	305	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523	PulA	1.90e-34	379	548	165	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11326	AmyAc_Glg_debranch	6.17e-34	380	548	10	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	1.99e-315	1	918	1	927
QIM10833.1	6.72e-272	23	918	10	908
QQR08212.1	7.65e-226	17	789	23	730
ANU64421.1	7.65e-226	17	789	23	730
ASB37479.1	7.65e-226	17	789	23	730

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4J7R_A	2.13e-24	332	586	158	456	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	1.40e-22	385	552	100	257	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	1.40e-22	385	552	100	257	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	1.40e-22	385	552	100	257	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	4.34e-22	385	552	100	257	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O22637	2.91e-25	320	565	172	437	Isoamylase SU1, chloroplastic OS=Zea mays OX=4577 GN=SU1 PE=1 SV=1
Q9M0S5	7.70e-24	332	552	184	433	Isoamylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA3 PE=1 SV=2
B9G434	5.07e-22	368	552	226	450	Isoamylase 3, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA3 PE=2 SV=1
Q55088	7.69e-22	385	552	101	258	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
O04196	8.82e-22	327	574	167	436	Isoamylase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA1 PE=1 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
0.000332	0.998999	0.000171	0.000163	0.000153	0.000142

TMHMM  Annotations     

start	end
7	29