CAZyme Information: MGYG000000369_00834

Basic Information

• Species: CAG-170 sp003516765
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-170; CAG-170 sp003516765
• CAZyme ID: MGYG000000369_00834
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
773	MGYG000000369_8|CGC1	88005.08	5.8066

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000369	1959873	MAG	Sweden	Europe

• Gene Location: Start: 42334; End: 44655 Strand: +

Full Sequence      

MSNEVERIVQQTEALLRLRHEETLQETTPQRLHECLGEVIMMQINDSWVKTKKRQTAGRR
AFYFSAEYLVGRLVYSNLFNLGILSEVKKAFAEKGVDLACLEEIEDAALGNGGLGRLAAC
FLDSAATCDVPLTGYGLRYRFGLFKQSFENGSQRENADDWTKFGDPWSHRRDKLAVKVNF
ANQTVIAVPYDMPVIGYENNTIGTLRLWQCEAEKELDFDAFNAQNYVKALETKNKAEDIT
RVLYPNDSTWEGKQLRIKQQYVLSSASLQDILRSFRENHGCDYYRLPEFDAVQLNDTHPA
MAIPELIRLLQLEGMDFESAFQIAARVFSYTNHTVMGEALEKWDLELLRSVVPEICDILE
KIDTRLKKEHPDSGLFIIKDHQAHMANLSVYVSTAVNGVARIHSEILKNDLFKDWYRYYP
ERFQNKTNGITPRRWLGLCNPELCGLIESKVGTGFLTDLDKLEGLKNGLDEMTVKQFNAI
KLEKKRQLCAVIEEHEGVKLDPSFVFDVQVKRLHEYKRQLMNALSIMDLYFGIKDGTISD
FTPTAFIFGAKAAPGYVRAKAIIRYINRVAELVNNDPAVADKMKVVFVQNYNCSYAEHII
PAADISEQISPAGTEASGTGNMKLMLNGAVTLGTMDGANVEIVERAGLENNYIFGASVEE
LNDIRESYCARDVYHSNPRIKRAVDTLVDGTVPTDSELRELYTSLLDGASWHRPDHYFVL
KDLPSYQQARLQANYDYRDRVEFGRKCLMNVASAGYFSSDRTIRQYAKEIWKI

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	90	773	1.8e-247	0.9970326409495549

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	48	773	57	810	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	22	773	23	748	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	24	772	26	795	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	23	773	12	794	glycogen/starch/alpha-glucan phosphorylases. This family consists of phosphorylases. Members use phosphate to break alpha 1,4 linkages between pairs of glucose residues at the end of long glucose polymers, releasing alpha-D-glucose 1-phosphate. The nomenclature convention is to preface the name according to the natural substrate, as in glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, etc. Name differences among these substrates reflect differences in patterns of branching with alpha 1,6 linkages. Members include allosterically regulated and unregulated forms. A related family, TIGR02094, contains examples known to act well on particularly small alpha 1,4 glucans, as may be found after import from exogenous sources. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
cd04300	GT35_Glycogen_Phosphorylase	0.0	23	773	15	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTE68668.1	0.0	8	773	6	779
QUC67788.1	0.0	8	773	6	779
QUA53587.1	0.0	8	773	6	779
QTE75423.1	0.0	8	773	6	779
QTE71458.1	0.0	8	773	6	779

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C4M_A	6.31e-249	36	773	37	788	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]
5IKO_A	2.00e-222	28	773	51	831	Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
1Z8D_A	2.61e-216	28	773	48	828	ChainA, Glycogen phosphorylase, muscle form [Homo sapiens]
2FFR_A	9.72e-215	28	773	36	816	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
5OX0_A	4.87e-214	28	773	48	828	GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9XTL9	2.57e-222	48	773	68	828	Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
P11216	9.97e-222	28	773	48	828	Glycogen phosphorylase, brain form OS=Homo sapiens OX=9606 GN=PYGB PE=1 SV=5
Q8CI94	5.64e-221	28	773	48	828	Glycogen phosphorylase, brain form OS=Mus musculus OX=10090 GN=Pygb PE=1 SV=3
Q5R5M6	1.60e-220	28	773	48	828	Glycogen phosphorylase, brain form OS=Pongo abelii OX=9601 GN=PYGB PE=2 SV=3
P53534	3.85e-220	28	773	48	828	Glycogen phosphorylase, brain form (Fragment) OS=Rattus norvegicus OX=10116 GN=Pygb 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
1.000075	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000369_00834.