CAZyme Information: MGYG000003782.1_01208

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus
• CAZyme ID: MGYG000003782.1_01208
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
275	MGYG000003782.1_267|CGC1	32732.91	5.1018

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003782.1	1597372	MAG	Canada	North America

• Gene Location: Start: 1671; End: 2498 Strand: -

Full Sequence      

MCLPIEYGGIGFDYRLAMGMPDFWEKSLEKQDEDWDLSKMWYELSTHRPEEKRVSYVESH
DQALVGSKTTIFRLADQEMYWNMRKDDHNMIIDRAIALHKMIRWITLSMGADAYLNFMGN
EFGHPEWIDFPREGNGYSYHYARRQWSLADSKDLKYQFLNNFDNAMIEFSKENCQLANET
YRLWIDNDRKIIAFRNKDIVYIFNFHPENSYESFQLPIHDIGEFKVLMDTDEGRFGGFDR
ISHEFTYQSEKLSGTDYDGIKIYIPSRTALALKKI

Enzyme Prediction     

EC	2.4.1.18

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1	120	2.3e-49	0.40955631399317405

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PLN02447	PLN02447	8.24e-110	2	269	454	725	1,4-alpha-glucan-branching enzyme
cd11321	AmyAc_bac_euk_BE	2.43e-100	1	163	241	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	4.57e-56	1	269	618	886	alpha-amylase
PLN03244	PLN03244	2.42e-54	1	273	593	865	alpha-amylase; Provisional
COG0296	GlgB	1.90e-20	2	273	365	627	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACV28257.1	2.30e-200	1	275	388	662
QQN56742.1	2.19e-155	1	275	388	662
QQB62075.1	2.19e-155	1	275	388	662
AHM57920.1	4.83e-125	1	275	403	679
AEV69892.1	1.96e-122	1	275	397	672

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5CLT_A	1.11e-79	1	275	388	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]
4BZY_A	2.17e-79	1	275	420	698	Crystalstructure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_B Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_C Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens]
3AMK_A	1.16e-72	1	275	407	693	Structureof the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
3VU2_A	1.16e-72	1	275	407	693	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]
7ML5_A	2.24e-72	1	275	406	692	ChainA, Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic [Oryza sativa Japonica Group]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q6CCT1	6.77e-84	1	274	406	684	1,4-alpha-glucan-branching enzyme OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=GLC3 PE=3 SV=1
Q8NKE1	1.22e-82	1	272	405	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
Q6T308	5.71e-79	1	275	417	695	1,4-alpha-glucan-branching enzyme OS=Felis catus OX=9685 GN=GBE1 PE=2 SV=1
Q04446	1.19e-78	1	275	420	698	1,4-alpha-glucan-branching enzyme OS=Homo sapiens OX=9606 GN=GBE1 PE=1 SV=3
Q9D6Y9	3.27e-78	1	275	420	698	1,4-alpha-glucan-branching enzyme OS=Mus musculus OX=10090 GN=Gbe1 PE=1 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
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003782.1_01208.