CAZyme Information: MGYG000004116_01299

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1591
• CAZyme ID: MGYG000004116_01299
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
777	MGYG000004116_6|CGC2	87975.39	5.344

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004116	3787047	MAG	United Kingdom	Europe

• Gene Location: Start: 25696; End: 28029 Strand: +

Full Sequence      

MKSLQEQIDRILEEDYQQRIETASTVQLYQAVSRAAMHQLASGGATPTDGKRVGYFSAEF
LMGRMIYANLLNLGILEEVRDLLAARGVDIGIFEEIEDAALGNGGLGRLAACFLDSAATQ
GIPLDGYGIRYRYGLFKQTFENGFQQESADDWTRFGDPWSVRREEDTVQVSFRGETVNAV
PYDMPIIGFGGKTVNTLRLWQAEAIKPFDFQLFNAQKYAAAVRERDKAEAISSVLYPNDN
TDPGKRLRLKQQYFFSSASLQDILRKYRRTGNEMTRLADKVAIQLNDTHPTVSIPELIRL
LCEEDGMPFEKALETAKAVFAYTNHTIMPEALERWNASLFRSVLPKVYPYVLRIDEALKK
DLTAAGFEGEAQKAYRIVDGDTIHMARLAIYATHSTNGVARLHTEILKRDALPEWYALFP
ERFNNKTNGITQRRWLALANPELSALVTEAVGPEWITDLDRLKGLENYRDDGSYLDRFAA
VKTRKKEQLAAFIQQQEGIQVPSSFLFDVQVKRLHEYKRQLLNAFSILDTYYGLKDGQIT
DFTPTLYLFGAKAAPGYFRAKGIIKYIHEVGRLINSDPDVADRMRVVFVHNYNVSYAEKI
IPAADVSQQISTAGTEASGTSNMKFMLNGAVTLGTYDGANVEIVQQAGEENNYIFGARVE
EIESLRDSYDPRALLEREPRIRRVVDSLVDGTFSDGGTGMFQDLYASLLEGASWHRPDNY
FLLYDFLPYCDARLRTNRDYADRRTFTQKCLMNTANAGIFSSDRTIQEYARDIWQVT

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	87	776	8.9e-256	0.9896142433234422

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	49	776	68	810	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	2	776	7	748	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	27	775	33	795	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	8	776	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	5	776	1	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
ADU28082.1	0.0	23	776	23	777
AYF39756.1	0.0	23	776	23	777
AVQ97094.1	0.0	23	776	23	777
AYF42589.1	0.0	23	776	23	777
QCN93337.1	0.0	23	776	23	777

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C4M_A	5.30e-254	23	776	28	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	7.36e-221	49	776	82	831	Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
5OX0_A	3.42e-218	49	776	79	828	GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]
2GJ4_A	5.27e-218	49	776	67	816	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2FFR_A	5.44e-218	49	776	67	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
Q8CI94	2.86e-222	49	776	79	828	Glycogen phosphorylase, brain form OS=Mus musculus OX=10090 GN=Pygb PE=1 SV=3
P53534	1.10e-220	49	776	79	828	Glycogen phosphorylase, brain form (Fragment) OS=Rattus norvegicus OX=10116 GN=Pygb PE=1 SV=3
Q3B7M9	1.83e-220	49	774	79	826	Glycogen phosphorylase, brain form OS=Bos taurus OX=9913 GN=PYGB PE=2 SV=3
P11216	3.66e-220	49	776	79	828	Glycogen phosphorylase, brain form OS=Homo sapiens OX=9606 GN=PYGB PE=1 SV=5
P79334	5.01e-220	49	776	79	828	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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004116_01299.