CAZyme Information: MGYG000000759_01647

Basic Information

• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium
• CAZyme ID: MGYG000000759_01647
• CAZy Family: GT35
• CAZyme Description: Glycogen phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
276		30779.74	4.6724

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000759	1836417	MAG	Bangladesh	Asia

• Gene Location: Start: 1349; End: 2179 Strand: -

Full Sequence      

MQIKRLHEYKRQLMNALYVLDLYFRIKERGETVPKRTFIFGAKAAPGYDRAKAIIKLINT
IADLVNNDPATKDIIRVVFVENYNVSPAEHIIPAADISEQISVAGKEASGTSNMKFMMNG
ALTLGTMDGANVEIVEAVGEDNAYIFGARNEELPQLRAEYNPGELYQSVPGLARVLDALV
DGTLGSENAGLFSDLRASLLDGYGEHAQDQYYVLGDFADYRETRDRMAAEYEADQLAWAK
KAWLNICYSGRFSSDRTIADYANEVWKIQPTPISQS

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	1	269	3.6e-96	0.37388724035608306

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00343	Phosphorylase	3.90e-165	2	268	400	661	Carbohydrate phosphorylase. The members of this family catalyze the formation of glucose 1-phosphate from one of the following polyglucoses; glycogen, starch, glucan or maltodextrin.
cd04300	GT35_Glycogen_Phosphorylase	1.25e-154	1	268	532	795	glycogen phosphorylase and similar proteins. This is a family of oligosaccharide phosphorylases. It includes yeast and mammalian glycogen phosphorylases, plant starch/glucan phosphorylase, as well as the maltodextrin phosphorylases of bacteria. The members of this family catalyze the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism. The allosteric control mechanisms of yeast and mammalian members of this family are different from that of bacterial members. The members of this family belong to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
COG0058	GlgP	2.08e-114	1	270	491	750	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	5.21e-98	2	269	534	797	maltodextrin phosphorylase; Provisional
PRK14986	PRK14986	1.07e-93	1	270	547	812	glycogen phosphorylase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQU82019.1	8.02e-184	2	275	522	795
QQA98249.1	1.83e-182	2	275	522	795
QQN48647.1	9.55e-180	2	274	522	794
QRQ66260.1	5.43e-179	2	274	522	794
QQU94609.1	8.01e-176	2	274	522	794

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C4M_A	2.64e-144	2	272	521	792	Starchphosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_B Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_C Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_D Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae]
2GJ4_A	4.84e-79	2	271	555	819	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A	4.92e-79	2	271	555	819	Structureof rabbit muscle glycogen phosphorylase in complex with thienopyrrole [Oryctolagus cuniculus],5MCB_A Glycogen phosphorylase in complex with chlorogenic acid. [Oryctolagus cuniculus],7ONF_A Chain A, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]
2FFR_A	4.92e-79	2	271	555	819	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
1ABB_A	5.15e-79	2	271	557	821	ControlOf Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_B Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_C Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_D Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P79334	1.28e-78	2	271	567	831	Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
P00489	3.53e-78	2	271	567	831	Glycogen phosphorylase, muscle form OS=Oryctolagus cuniculus OX=9986 GN=PYGM PE=1 SV=3
O18751	4.86e-78	2	271	567	831	Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
P11217	9.44e-78	2	271	567	831	Glycogen phosphorylase, muscle form OS=Homo sapiens OX=9606 GN=PYGM PE=1 SV=6
Q9WUB3	1.32e-77	2	271	567	831	Glycogen phosphorylase, muscle form OS=Mus musculus OX=10090 GN=Pygm PE=1 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
1.000058	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000759_01647.