CAZyme Information: MGYG000002807_00420

Basic Information

• Species: Eubacterium_R sp900539165
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900539165
• CAZyme ID: MGYG000002807_00420
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
848		95573.35	6.9313

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002807	1764558	MAG	Peru	South America

• Gene Location: Start: 52953; End: 55499 Strand: -

Full Sequence      

MKTSISTSQAKRLITDKLSHFFGVSPSDATDEQFYKAVAMIVRDRLSEQNSEFRHIAKDQ
DSKQVYYLCMEFLMGRSLKNNLYNLGLASVFNDALASMGVKLDNLYELEPDAGLGNGGLG
RLAACYLDGLATDGFQSMGYSLRYEAGIFKQKLIDGWQTELPDFWLPGGEVWLVPREERA
CKVYFEGHIEDSWDGDFHHVAHKDANIVEAVPYDMYVSGKGEGVSRLRLWASKKPELDMA
LFNEGSYMKAMEQSAMAEAITKILYPADNSPEGKSLRLRQQYFLVSASIQDIIQRHLTKY
GTLDNLPDKVAIHINDTHPTMAIPELMRIMLDECGYGWDDAWSIVTRTVAYTNHTVMKEA
LECWSEELYSRLLPRIYQITKEIDNRFRAYIWSVTHDADRVERMAVVSNGVVRMANLCVI
GSHSVNGVSALHSEILKETVFNDFYNITPEKFTNVTNGIAFRRWICQANPELTDYISSLI
GDGFITKSDELLKLRKFADDKKVLARLDEIKHDNKVRFAKLIKKRNGIDVNPDSIFDVQV
KRLHEYKRQQLNVLNIISEYLMLKENPNADYYPKTYIFASKAAPGYFMAKKIIELIDALS
KVINNDPDVAGKLKVVFLEDYNVSLAEVLMPAADISEQISLAGTEASGTGNMKLMLNGAI
TLGTLDGANVEIFDAVGEDNICIFGMKTPEVNQLKNSGYNPQTYIQNNEALAKAMAFIQN
GVNGKKFDEIYYSLLNTDPYMALADFTDYQRAQQQISKAYADREKFVRMSLMNISGAGVF
SADRSIMDYANLIWHTKPVQFPKTEPKAEKKAPAKKAEPKAEKKAPAKKAEPKAEKKAPA
KSKAKSKK

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	94	796	1.8e-262	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	1	797	1	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	4	799	6	803
QKO30335.1	0.0	1	799	1	800
ARP49466.1	0.0	1	799	1	800
QKN23059.1	0.0	1	799	1	800
CAB1243764.1	0.0	1	799	1	800

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Z8D_A	3.38e-240	29	798	47	830	ChainA, Glycogen phosphorylase, muscle form [Homo sapiens]
2GJ4_A	6.81e-238	29	798	35	818	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A	7.04e-238	29	798	35	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	7.04e-238	29	798	35	818	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
7O8E_A	8.30e-238	29	798	40	823	ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P73511	1.81e-241	2	799	21	829	Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
P11217	2.31e-240	29	798	47	830	Glycogen phosphorylase, muscle form OS=Homo sapiens OX=9606 GN=PYGM PE=1 SV=6
Q8HXW4	1.85e-239	29	798	47	830	Glycogen phosphorylase, muscle form OS=Macaca fascicularis OX=9541 GN=PYGM PE=2 SV=3
P79334	1.68e-237	29	800	47	832	Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
Q9XTL9	1.80e-237	29	798	47	830	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
1.000069	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002807_00420.