CAZyme Information: MGYG000003172_01325

Basic Information

• Species: CAG-485 sp900555915
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900555915
• CAZyme ID: MGYG000003172_01325
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
220		25682.38	7.0752

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003172	1933519	MAG	United States	North America

• Gene Location: Start: 2144; End: 2806 Strand: -

Full Sequence      

MGDKTIIFRLIDKEMYWHMMVDDNNFTVERGMALHKMIRLVTLATINGGYLNFMGNEFGH
PEWIDFPREGNGWSHKYARRQWDLVDREDLKYKFLNAFDNSMISVVDKQYNFQAKPVEKL
WEKDDDQVLAFKRGDLIFVFNWSPNKSFDGYGFLAPAGEYEVVLDSDAKDFGGFGLVDDT
VHHFTTPDPLYSPAGKGWLKMYLPARTAQVLKMVRTRKKK

Enzyme Prediction     

EC	2.4.1.18

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PLN02447	PLN02447	2.14e-90	2	210	519	727	1,4-alpha-glucan-branching enzyme
cd11321	AmyAc_bac_euk_BE	8.03e-62	2	99	307	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	3.50e-44	30	215	710	893	alpha-amylase
PLN03244	PLN03244	7.21e-42	27	215	682	868	alpha-amylase; Provisional
pfam02806	Alpha-amylase_C	1.53e-13	124	212	7	91	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
ASB37969.1	1.78e-123	2	215	457	670
ANU63937.1	1.78e-123	2	215	457	670
QQR08704.1	1.78e-123	2	215	457	670
QCD39297.1	8.36e-117	2	220	457	675
QCP72988.1	8.36e-117	2	220	457	675

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7ML5_A	1.77e-60	2	188	472	660	ChainA, Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic [Oryza sativa Japonica Group]
3AMK_A	1.80e-60	2	188	473	661	Structureof the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
3VU2_A	1.80e-60	2	188	473	661	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	3.45e-60	2	188	473	661	Structureof the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
5CLT_A	1.24e-51	2	214	454	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	1.06e-60	2	188	558	746	1,4-alpha-glucan-branching enzyme OS=Solanum tuberosum OX=4113 GN=SBE1 PE=2 SV=2
Q01401	3.64e-59	2	188	538	726	1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic OS=Oryza sativa subsp. japonica OX=39947 GN=SBE1 PE=1 SV=2
Q41059	3.43e-56	2	188	538	727	1,4-alpha-glucan-branching enzyme 1, chloroplastic/amyloplastic (Fragment) OS=Pisum sativum OX=3888 GN=SBEII PE=1 SV=1
Q6CCT1	6.43e-55	2	210	472	681	1,4-alpha-glucan-branching enzyme OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=GLC3 PE=3 SV=1
Q9Y8H3	1.14e-53	2	216	469	683	1,4-alpha-glucan-branching enzyme OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=be1 PE=2 SV=3

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
1.000067	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003172_01325.