CAZyme Information: MGYG000003925_02147

Basic Information

• Species: CAG-882 sp900545175
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-882; CAG-882 sp900545175
• CAZyme ID: MGYG000003925_02147
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
646	MGYG000003925_30|CGC2	73943.9	5.4398

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003925	3268447	MAG	China	Asia

• Gene Location: Start: 24703; End: 26643 Strand: +

Full Sequence      

MGISYRACREDRDFKKINGKLCEYMKIPDKSSITLEAASDISPGAKRITRGWQFGIFSND
TVMMLTLFLQNEPDNCISVEIPGTFRKGNFFSFILEFADESGADELDGVCYAVGEEKRAD
VYAKEYCYAAKEAERGGDFFGRSRDELYSVLRCDIPMEKNRESSIYDTLCSSENITAPLI
YKLHVRGYTKLESENGGTFAALMKKAEYIQELGMNMVLLMPCYEFNETTVSAERNNYYDA
GFASGKINYWGYTDGYYFAPKRAYCAGGNCVEEFGRMVNLFHEKSIAVLMEMWFPYDMSP
VMAVEILRYWHITYGIDGFRIMGSCGLLYAVRTDMQLADCVLLGEDFGEDSFNVGAVQPF
YDDKRRIIKYNDGFMEAGRHFLRGDEDSIVNFVNRVTRHDGGHPTVNFMADQNCLSLMDM
VSFERRHNEYNGENNLDGRRYNISFNCGTEGKTKREVILRQRKKMIKNALAMVFLSASVP
MLMAGDEFGVSHGGNNNPYCHDNDINYIDWELLSKNSDLYEFTRKLIQFRKEHSCIRPQH
DFSMNDHKIKGMPDLSCHSERAWFPLMAEYSHNIGLLYSGAYAGEQANVYVLYNMHTQLH
EFAVIEMAGKKWTCALSSDETGVVYDENRKKIKLAPYTMAVFVSQI

Enzyme Prediction     

No EC number prediction in MGYG000003925_02147.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	302	489	4.2e-38	0.5811965811965812

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11326	AmyAc_Glg_debranch	6.00e-100	180	533	18	433	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.
COG1523	PulA	5.41e-72	179	646	173	693	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PRK03705	PRK03705	1.33e-54	180	531	153	559	glycogen debranching protein GlgX.
PRK14510	PRK14510	6.65e-51	180	543	161	578	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11341	AmyAc_Pullulanase_LD-like	2.82e-28	176	530	1	406	Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of 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
AOZ96349.1	2.83e-110	65	636	40	623
ADL06627.1	3.18e-105	44	621	17	578
QRV19300.1	3.18e-105	44	621	17	578
ASN98292.1	6.08e-105	44	645	18	617
QRP36901.1	6.08e-105	44	645	18	617

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VNC_A	6.83e-44	179	553	175	609	Crystalstructure of Glycogen Debranching enzyme TreX from Sulfolobus solfataricus [Saccharolobus solfataricus],2VNC_B Crystal structure of Glycogen Debranching enzyme TreX from Sulfolobus solfataricus [Saccharolobus solfataricus],2VR5_A Crystal structure of Trex from Sulfolobus Solfataricus in complex with acarbose intermediate and glucose [Saccharolobus solfataricus],2VR5_B Crystal structure of Trex from Sulfolobus Solfataricus in complex with acarbose intermediate and glucose [Saccharolobus solfataricus],2VUY_A Crystal structure of Glycogen Debranching exzyme TreX from Sulfolobus solfatarius [Saccharolobus solfataricus],2VUY_B Crystal structure of Glycogen Debranching exzyme TreX from Sulfolobus solfatarius [Saccharolobus solfataricus],7EAV_A Chain A, Glycogen debranching enzyme [Saccharolobus solfataricus],7EAV_B Chain B, Glycogen debranching enzyme [Saccharolobus solfataricus]
4J7R_A	2.58e-43	179	612	225	774	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]
2WSK_A	1.09e-32	179	531	152	559	Crystalstructure of Glycogen Debranching Enzyme GlgX from Escherichia coli K-12 [Escherichia coli K-12]
6JHH_A	1.53e-12	176	537	154	565	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JEQ_A	1.53e-12	176	537	154	565	Crystalstructure of Pullulanase from Paenibacillus barengoltzii complex with beta-cyclodextrin [Paenibacillus barengoltzii],6JFJ_A Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltohexaose and alpha-cyclodextrin [Paenibacillus barengoltzii],6JFX_A Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltopentaose [Paenibacillus barengoltzii],6JHF_A Crystal structure of apo Pullulanase from Paenibacillus barengoltzii [Paenibacillus barengoltzii],6JHG_A Crystal structure of apo Pullulanase from Paenibacillus barengoltzii in space group P212121 [Paenibacillus barengoltzii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
D0TZF0	1.05e-46	179	532	246	680	Isoamylase 1, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA1 PE=1 SV=1
O22637	3.64e-45	179	612	231	735	Isoamylase SU1, chloroplastic OS=Zea mays OX=4577 GN=SU1 PE=1 SV=1
P0A4Y5	1.35e-44	179	542	174	599	Glycogen operon protein GlgX homolog OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=glgX PE=3 SV=1
P9WQ24	1.35e-44	179	542	174	599	Glycogen operon protein GlgX homolog OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=glgX PE=3 SV=1
P9WQ25	1.35e-44	179	542	174	599	Glycogen operon protein GlgX homolog OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=glgX 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
1.000003	0.000046	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003925_02147.