CAZyme Information: MGYG000001956_00105

Basic Information

• Species: Eubacterium_R sp900543795
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900543795
• CAZyme ID: MGYG000001956_00105
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
832		93383.69	6.2299

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001956	1751837	MAG	Denmark	Europe

• Gene Location: Start: 13674; End: 16172 Strand: +

Full Sequence      

MKSTISVAQAKKMIDDKLSHFFGVSPETASIEQYYKAVSMIVRDELQAASSDFRHIAKGQ
DSKTVYYLCMEFLMGRSLKNNLYNLGLTEVFNEALKGFDVSIEKLYEQEPDAGLGNGGLG
RLAACYLDGLATNGFQSMGYSIRYEAGIFKQKLVDGWQTELPDFWLPGGDVWLVPREERA
VEVKFEGWVDDSWDGDYHHVEQRDCNSVTAIPYDMYVSGAGKGVSRLRLWASRKPELDMS
LFNQGSFIKAMEQSAMAEAISKVLYPADNSPEGKSLRLRQQYFLVSASIQDIIQRHLTKY
GTLDNLPEKVAIHINDTHPTMAIPELMRIMLDECGYGWDDAWSIVTKTVAYTNHTVMKEA
LECWSEELYSRLLPRIYQITKEIDNRFRAYVWGVTHDADKVERMAIVSGGVVRMANLCVA
GSHSVNGVSALHSEILKETVFNDFYTITPDKFTNVTNGIAFRRWLCQANPALTKYITELI
GDGFITKSDELIKLRDFKDDKQVLADLAEIKRQNKVRFAELVKKRNGVEINPDSIFDVQV
KRLHEYKRQSLNILNIIAEYQMIKANPSVDFEPRTYIFASKAAPGYYMAKKTIELIDALS
KLINNDPDVNGKIKVVFMEDYNVSLAEVLMPAADISEQISLAGTEASGTGNMKLMLNGAI
TLGTLDGANVEIAQAVGNDNIIIFGMKTPEVQQLQRDGYYPMNYINNNPALKGVIDFLNM
GVNGKSFGEITSSLMNVDPYMALADFADYQKAQAFSAEVYRDKERFARMSLMNISGAGVF
SADRSIMDYANNIWHTKPVQFPEEAKKPVNAEGASVKKAQKKTASKKKTAKK

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	94	796	1e-258	0.9970326409495549

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	4	800	11	814	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	2	798	1	750	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	33	797	33	797	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	14	796	1	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	11	795	1	794	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
BCI59382.1	0.0	1	804	3	808
QKO30335.1	0.0	6	799	6	800
ARP49466.1	0.0	6	799	6	800
QKN23059.1	0.0	6	799	6	800
CAB1239238.1	0.0	7	806	7	807

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Z8D_A	3.15e-239	6	805	24	841	ChainA, Glycogen phosphorylase, muscle form [Homo sapiens]
2GJ4_A	5.60e-238	6	798	12	818	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A	5.79e-238	6	798	12	818	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	5.79e-238	6	798	12	818	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
7O8E_A	6.82e-238	6	798	17	823	ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P79334	1.52e-239	6	800	24	832	Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
O18751	2.15e-239	6	800	24	832	Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
P11217	2.15e-239	6	805	24	841	Glycogen phosphorylase, muscle form OS=Homo sapiens OX=9606 GN=PYGM PE=1 SV=6
Q3B7M9	4.45e-239	7	798	25	830	Glycogen phosphorylase, brain form OS=Bos taurus OX=9913 GN=PYGB PE=2 SV=3
Q9XTL9	1.30e-238	6	810	24	844	Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2

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
1.000039	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001956_00105.