CAZyme Information: MGYG000000718_00003

Basic Information

• Species: SFDB01 sp004558825
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-138; SFDB01; SFDB01 sp004558825
• CAZyme ID: MGYG000000718_00003
• CAZy Family: GT35
• CAZyme Description: Glycogen phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
789		90647.34	6.6262

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000718	1975049	MAG	Kazakhstan	Asia

• Gene Location: Start: 1724; End: 4093 Strand: +

Full Sequence      

MLMDSKAILRRMEDELNSEYQIELTEATAQQLHRALSNAVMFAVSDDWRRSRREHERVRR
AYYFSAEYLMGRMIYNNLYCLGILDDIKRYLLVRGADISKFEDIEDAALGNGGLGRLAAC
FLDSAATHDLPLDGYGLRYKFGLFKQRFENGFQIEKADNWQRYGDPWSRRRDDKTVTVNF
AGQSVLAVPYDMPIIGYDTTNIGTLRLWQSEPIEEFDFNLFNDQQYAMSVREKNSVEDIT
RVLYPNDSTDEGKRLRLKQQYFLSSASIQDIIRRYKRTRGSDFSFFAAHCAIQLNDTHPT
VSIPELIRLLMLENMDFPTALNVARSVFSYTNHTIMNEALERWNIGLMRSVIPEICDIIC
RIDDMLVNELMSRGVGAEQIDRMRIIDNGTVHMARLATYVSRYVNGVARIHTEILKHDIL
KDWYSIYPERFQNKTNGITQRRWLGLCNEELTFLIKEKIGDGFLRDLSQLERLKPLIDDD
MISRFIEIKRIKKQQLCGVINKREGFLLNPAFIFDVQVKRMHEYKRQLMNAFSVAHIYFM
LKDGALPAFTPTAFIFGAKAAPGYYRAKGIIKYINELAAMINADRDVRDKMQVVFVQNYN
CSYAEHIIPAADISEQISPAGTEASGTGNMKFMLNGTVTLGTFDGANIEIADAAGVENNY
IFGATVDDIARIAPLYDPKRLYDENPDIRRVVDTLIDGSLSDGGTGVFRELYNSLLYGAS
WHRADNYFVLLDLPPYIEAKLRANRDYQDKYSFARKSLINAASAGRFSSDRTVAEYARDI
WHIESIKGK

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	95	784	9.5e-248	0.9910979228486647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	38	787	43	814	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	10	784	11	749	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	24	781	26	794	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	12	783	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	10	783	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
QCT06755.1	0.0	7	784	2	785
CBL34093.1	0.0	19	786	17	786
CBK95778.1	0.0	19	786	17	786
BCN32947.1	0.0	16	783	16	781
CDZ24764.1	0.0	8	786	507	1285

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C4M_A	4.44e-248	27	784	28	789	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	1.60e-217	27	784	50	832	Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
1Z8D_A	5.72e-214	27	784	47	829	ChainA, Glycogen phosphorylase, muscle form [Homo sapiens]
2FFR_A	6.66e-214	27	784	35	817	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
5OX0_A	8.35e-214	27	784	47	829	GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q3B7M9	2.20e-219	27	784	47	829	Glycogen phosphorylase, brain form OS=Bos taurus OX=9913 GN=PYGB PE=2 SV=3
Q8CI94	3.11e-219	27	784	47	829	Glycogen phosphorylase, brain form OS=Mus musculus OX=10090 GN=Pygb PE=1 SV=3
Q9XTL9	2.05e-217	27	784	47	829	Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
Q5MIB6	3.97e-217	27	784	47	829	Glycogen phosphorylase, brain form OS=Ovis aries OX=9940 GN=PYGB PE=2 SV=3
P11216	7.95e-217	27	784	47	829	Glycogen phosphorylase, brain form OS=Homo sapiens OX=9606 GN=PYGB PE=1 SV=5

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
1.000036	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000718_00003.