dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002815_01122

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Basic Information help

Species

Anaerococcus prevotii_A

Lineage

Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus; Anaerococcus prevotii_A

CAZyme ID

MGYG000002815_01122

CAZy Family

GT35

CAZyme Description

Glycogen phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
751	MGYG000002815_5\|CGC1	88324.53	5.5017

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002815	1697277	MAG	United States	North America

Gene Location

Start: 117477; End: 119732 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002815_01122.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT35	94	744	3.8e-127	0.9807121661721068

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04300	GT35_Glycogen_Phosphorylase	1.48e-124	19	732	7	773	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	1.45e-92	94	732	1	639	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	1.03e-80	10	732	11	726	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14986	PRK14986	1.56e-80	63	744	71	800	glycogen phosphorylase; Provisional
PRK14985	PRK14985	1.03e-51	55	731	52	773	maltodextrin phosphorylase; Provisional

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACV28899.1	0.0	1	751	1	752
QQB62731.1	1.44e-254	7	741	3	742
QQN55753.1	4.10e-254	7	741	3	742
QUY64655.1	3.61e-114	7	691	2	690
QZO77069.1	1.39e-113	7	691	2	690

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2FFR_A	1.51e-67	7	744	11	806	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
4Z5X_A	2.64e-67	7	744	23	818	Glycogenphosphorylase in complex with gallic acid [Oryctolagus cuniculus]
2GJ4_A	2.81e-67	7	744	11	806	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A	2.85e-67	7	744	11	806	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]
4EJ2_A	2.85e-67	7	744	11	806	Crystalstructure of GPb in complex with DK10 [Oryctolagus cuniculus],4EKE_A Crystal structure of GPb in complex with DK11 [Oryctolagus cuniculus],4EKY_A Crystal structure of GPb in complex with DK15 [Oryctolagus cuniculus],4EL0_A Crystal structure of GPb in complex with DK16 [Oryctolagus cuniculus],4EL5_A Crystal structure of GPb in complex with DK12 [Oryctolagus cuniculus],4MHO_A Crystal structure of Gpb in complex with S3, SUGAR (N-[(BIPHENYL-4-YLOXY)ACETYL]-BETA-D-GLUCOPYRANOSYLAMINE) [Oryctolagus cuniculus],4MHS_A Crystal structure of Gpb in complex with SUGAR (N-[(2E)-3-(BIPHENYL-4-YL)PROP-2-ENOYL]-BETA-D-GLUCOPYRANOSYLAMINE [Oryctolagus cuniculus],4MI3_A Crystal structure of Gpb in complex with SUGAR (N-{(2R)-2-METHYL-3-[4-(PROPAN-2-YL)PHENYL]PROPANOYL}-BETA-D-GLUCOPYRANOSYLAMINE) (S21) [Oryctolagus cuniculus],4MI6_A Crystal structure of Gpb in complex with SUGAR (N-[4-(5,6,7,8-TETRAHYDRONAPHTHALEN-2-YL)BUTANOYL]-BETA-D-GLUCOPYRANOSYLAMINE) [Oryctolagus cuniculus],4MI9_A Crystal structure of Gpb in complex with SUGAR (N-[(3R)-3-(4-ETHYLPHENYL)BUTANOYL]-BETA-D-GLUCOPYRANOSYLAMINE) (S20) [Oryctolagus cuniculus],4MIC_A Crystal structure of Gpb in complex with SUGAR (N-{(2E)-3-[4-(PROPAN-2-YL)PHENYL]PROP-2-ENOYL}-BETA-D-GLUCOPYRANOSYLAMINE) (S6) [Oryctolagus cuniculus],4MRA_A Crystal structure of Gpb in complex with QUERCETIN [Oryctolagus cuniculus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39123	7.16e-79	26	744	22	784	Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
P45180	9.28e-75	59	744	72	804	Glycogen phosphorylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=glgP PE=3 SV=1
Q9PKE6	3.31e-70	1	744	6	799	Glycogen phosphorylase OS=Chlamydia muridarum (strain MoPn / Nigg) OX=243161 GN=glgP PE=3 SV=1
O84250	8.79e-70	12	744	17	799	Glycogen phosphorylase OS=Chlamydia trachomatis (strain D/UW-3/Cx) OX=272561 GN=glgP PE=3 SV=1
P0AC87	1.58e-68	26	744	31	800	Glycogen phosphorylase OS=Shigella flexneri OX=623 GN=glgP PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000047	0.000004	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000002815_01122.