CAZyme Information: MGYG000003002_01443

Basic Information

• Species: Streptococcus sanguinis_H
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus sanguinis_H
• CAZyme ID: MGYG000003002_01443
• CAZy Family: GT35
• CAZyme Description: Glycogen phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
301		34524.19	4.8688

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003002	1839775	MAG	United States	North America

• Gene Location: Start: 6461; End: 7366 Strand: -

Full Sequence      

MLGDFYRVKQEAKARLADFIKESTGVEVSTEAIFDVQVKRLHAYKRQLLNLLHIIKLYWD
LKDNPNKDMVPRVFIFGAKAAPGYHFAKSVIKLINEVANLVNKDESLQGKLKVVFLENYR
VSLAELIIPAADVSEQISLASKEASGTSNMKFMMTGAITLATLDGANIEIKDEVGDDNIV
IFGMDKDQVYEHYARHDYYSRGVYESNPDIRRVVDTFVNGTIPNVREEGSEIYEALITHN
DEYFLLEDFHAYVEAQEKIDALYRDKEKWARMSLINIATSDKFTSDDTIEQYAREIWNLE
K

Enzyme Prediction     

No EC number prediction in MGYG000003002_01443.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	5	299	1.6e-113	0.41839762611275966

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04300	GT35_Glycogen_Phosphorylase	0.0	2	299	498	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.
pfam00343	Phosphorylase	0.0	5	299	368	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.
COG0058	GlgP	1.51e-124	8	301	463	750	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	7.68e-121	6	297	502	794	maltodextrin phosphorylase; Provisional
PRK14986	PRK14986	2.80e-107	8	300	519	811	glycogen phosphorylase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKQ44197.1	6.14e-207	1	301	498	798
SQG32651.1	2.47e-206	1	301	498	798
QGS43874.1	3.51e-206	1	301	498	798
VTS82745.1	3.51e-206	1	301	498	798
VEE22259.1	3.51e-206	1	301	498	798

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2GJ4_A	1.45e-89	2	300	520	817	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A	1.48e-89	2	300	520	817	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	1.48e-89	2	300	520	817	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
1ABB_A	1.56e-89	2	300	522	819	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]
1C50_A	1.62e-89	2	300	519	816	IdentificationAnd Structural Characterization Of A Novel Allosteric Binding Site Of Glycogen Phosphorylase B [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39123	1.36e-98	2	299	497	794	Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
Q9CN90	6.36e-91	7	299	523	814	Glycogen phosphorylase OS=Pasteurella multocida (strain Pm70) OX=272843 GN=glgP PE=3 SV=1
Q9XTL9	1.44e-90	7	300	537	829	Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
P09812	5.60e-89	2	300	532	829	Glycogen phosphorylase, muscle form OS=Rattus norvegicus OX=10116 GN=Pygm PE=1 SV=5
Q9ET01	6.44e-89	2	300	532	829	Glycogen phosphorylase, liver form OS=Mus musculus OX=10090 GN=Pygl PE=1 SV=4

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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003002_01443.