CAZyme Information: MGYG000004820_01886

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173
• CAZyme ID: MGYG000004820_01886
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
207		23894.29	9.5687

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004820	2422420	MAG	China	Asia

• Gene Location: Start: 1170; End: 1793 Strand: -

Full Sequence      

MMVGDDNMTVARGMALHKMIRLVTLATINGGYLNFMGNEFGHPEWIDFPREGNGWSYKYA
RRQWDLVDREDLQYKFLNAFDNAMISLVSGVANFQSLGIEKLWEKDSDQVLAFRRGNFVF
VFNFSPTRSFTDYGVLTPPGKYRVVLSTDNPKFGGYGNIDEKVDHLTQYDELYAPIGKEW
LKLYLPARSAQVLRLVRQRPKKTTTNK

Enzyme Prediction     

EC	2.4.1.18

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PLN02447	PLN02447	2.05e-82	4	196	540	731	1,4-alpha-glucan-branching enzyme
cd11321	AmyAc_bac_euk_BE	1.36e-49	1	81	324	405	Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. 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.
PLN02960	PLN02960	2.67e-48	12	197	710	893	alpha-amylase
PLN03244	PLN03244	4.37e-43	9	197	682	868	alpha-amylase; Provisional
pfam02806	Alpha-amylase_C	3.02e-15	106	196	7	93	Alpha amylase, C-terminal all-beta domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCD43612.1	6.95e-108	1	204	474	677
QCD39297.1	5.35e-107	1	202	474	675
QCP72988.1	5.35e-107	1	202	474	675
QCD36412.1	3.47e-102	1	194	472	665
ASB37969.1	1.49e-98	4	199	477	672

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7ML5_A	2.79e-49	9	167	498	657	ChainA, Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic [Oryza sativa Japonica Group]
3AMK_A	2.81e-49	9	167	499	658	Structureof the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
3VU2_A	2.81e-49	9	167	499	658	Structureof the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L [Oryza sativa Japonica Group],3VU2_B Structure of the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L [Oryza sativa Japonica Group]
3AML_A	4.22e-49	9	167	499	658	Structureof the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
5CLT_A	3.51e-45	12	196	483	666	Crystalstructure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLW_A Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P30924	2.07e-48	5	167	580	743	1,4-alpha-glucan-branching enzyme OS=Solanum tuberosum OX=4113 GN=SBE1 PE=2 SV=2
Q01401	3.32e-48	9	167	564	723	1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic OS=Oryza sativa subsp. japonica OX=39947 GN=SBE1 PE=1 SV=2
Q8NKE1	3.35e-47	12	193	500	680	1,4-alpha-glucan-branching enzyme OS=Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194) OX=747089 GN=GLC3 PE=2 SV=2
Q41059	3.92e-46	9	167	564	724	1,4-alpha-glucan-branching enzyme 1, chloroplastic/amyloplastic (Fragment) OS=Pisum sativum OX=3888 GN=SBEII PE=1 SV=1
Q6BXN1	2.02e-45	12	195	517	706	1,4-alpha-glucan-branching enzyme OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=GLC3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000084	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004820_01886.