CAZyme Information: MGYG000002260_00269

Basic Information

• Species: Eubacterium_R sp900540235
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900540235
• CAZyme ID: MGYG000002260_00269
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
780	MGYG000002260_2|CGC1	89817.47	5.0446

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002260	2117574	MAG	Peru	South America

• Gene Location: Start: 93528; End: 95870 Strand: +

Full Sequence      

MENIKEKLELLSFGKYNKNVENLNANELYDVVSTCVISAVSSSWQKSYEKHLKSRRACYF
SAEYLVGQPLYKNLMCLDLLKPFEDALSSFNRSLSEFETVPDELLGNGGLGRLAACFLDS
GANLSLPLDGYGIKYKFGLFKQKIENGFQLEDIENVDYSDSWCVPCFDDRAVVHFKEYDV
YAIPYDMPIVAYGSEHFSTLRLWQCEPIKEFDFKLFNEQKYDLALKQKNDAENISRLLYP
NDSTPDGKKLRFKQQYFFTCASLQDIIKKYKKYHCDDYCHFAEYITIQLNDTHPVVAIPE
LIRLLTLDGCTFDYAFDICCRVFNFTNHTIMAEALEKWDLNLIDDICPDIARIIINIDKK
QAKELSNENSDIQIIQNGMVHMANLACFVCKYINGVANLHTQILKSDTLNSWYKLTPNKF
QNKTNGITQRRFLRLCNPKLSELITDLLGSEEWINDLSKLKELEKFADNKDVLDRFMDIK
KENKKTLSNYILKLDNDSFSPDFIVDSQIKRLHEYKRQFLNILVILELYFELEEKSLTDF
TPTVFIFGAKSAPGYERAKGIIKLINEVKRLVEANEYVSRFIKIIFVSDYSVSYAEKIIP
ATDISKQISTAGTEASGTGNMKFMLNGAVTLGTFDGANIEIVQNAGEENNYIFGARVEDI
EKIKSTYDPKKIYNSDPKIKRCLDALVNGTLSDNNTGIFKELYTSILDGASWHKADNYYL
LLDFEPMLQTQLKANNDFKDKYDFAHKCFLNMCNAGFFSSDRTILDYAENIWDITKTDEI

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	87	774	2.2e-229	0.9955489614243324

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	44	774	57	810	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	1	774	10	748	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	55	772	59	794	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	4	774	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	2	774	2	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
CCO05339.1	5.39e-301	15	774	17	788
CBL34863.1	5.03e-297	2	774	10	790
ADU23251.1	5.39e-297	12	774	17	787
CBK96326.1	2.88e-296	2	774	10	790
BCJ96995.1	6.63e-296	3	774	4	779

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C4M_A	2.01e-233	32	777	37	791	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]
1Z8D_A	6.52e-177	45	774	73	828	ChainA, Glycogen phosphorylase, muscle form [Homo sapiens]
5OX0_A	1.49e-175	45	774	73	828	GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]
2GJ4_A	2.38e-175	45	774	61	816	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2FFR_A	2.45e-175	45	774	61	816	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9Z8N1	1.54e-182	21	774	34	814	Glycogen phosphorylase OS=Chlamydia pneumoniae OX=83558 GN=glgP PE=3 SV=1
Q9XTL9	2.47e-180	17	777	43	831	Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
P73511	6.35e-179	26	774	51	826	Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
O84250	2.49e-178	21	776	30	811	Glycogen phosphorylase OS=Chlamydia trachomatis (strain D/UW-3/Cx) OX=272561 GN=glgP PE=3 SV=1
P79334	3.21e-177	45	777	73	831	Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM 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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002260_00269.