CAZyme Information: MGYG000001424_00480

Basic Information

• Species: Anaerococcus senegalensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus; Anaerococcus senegalensis
• CAZyme ID: MGYG000001424_00480
• CAZy Family: GT35
• CAZyme Description: Glycogen phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
751	MGYG000001424_1|CGC3	89775.8	6.898

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001424	1780318	Isolate	not provided	not provided

• Gene Location: Start: 462089; End: 464344 Strand: -

Full Sequence      

MKKENNFILKRIQNFLYSFYAKDIKEARLSEIYDGLVKALMQDIGKNWSKSKKNFKSKEV
YILSFEYNPGKFLSNAIDSLNYQDEVRECLSILNISMSDLIKYEKEASLGISEIGTGAWY
LSKQLSENKIKSLSYALRYESGGMKQKIMNGIQLIDSNEWLYKGNKWEHKKAFSYLINIG
DKKLKSVAYDMPIYNNENDFVNTLRLWKAESINKINYSNNISSDFKKYYEDYIDNNSLTQ
FLYLDNSTYEGKLFRLKQEYFYCVSTIQDIFRRYFKNNDNIEKIYEKIKIILCDIHPSLA
IIEFIRCLHFGYDLDLEKCVEICKKVFDHIAFLVTPDSKEYYDMSMIKLVDISLYNIILK
LDSYAKNNLNVNIIENDQIKYNKINYYFVDEYFYLSKIIVDNDKDFIQDFSTLDFGIDRY
MYSQSRNINLKEILKKYNIDILENNNLEKLKDLKGNLEFYNDIDIMKYNNKIKFIDYFNL
DRNNSINPYSIFDMQLSMFHEAKRQLLNAITIASTYYMLKENSNIFITPTTYIFSGKASD
SYYMAKEIIKFIFALKHMIDKDRLIKEKIKIIFIEDLNVEKLKKIYPACDIYSHLTLPIY
DNQSFDMLNSIFNFSNIVSSKAGVLNNINSPNKIYKFGKEYEEIIKVQNENLYDAREFYY
KNDIIRHTVDNLINEDYNTLPYNFKNIYDYILSYNDSFFVFNDNQELFNIRSIISRDYLD
KNKWIDNEIDNILWAKEFKFRNYLEKFKKEI

Enzyme Prediction     

No EC number prediction in MGYG000001424_00480.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	91	751	4.6e-109	0.9896142433234422

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04300	GT35_Glycogen_Phosphorylase	1.43e-100	10	732	2	773	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.
pfam00343	Phosphorylase	9.05e-69	135	724	46	631	Carbohydrate phosphorylase. The members of this family catalyze the formation of glucose 1-phosphate from one of the following polyglucoses; glycogen, starch, glucan or maltodextrin.
PRK14986	PRK14986	1.06e-61	59	732	71	788	glycogen phosphorylase; Provisional
COG0058	GlgP	2.90e-54	13	732	11	726	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	1.38e-41	60	591	61	630	maltodextrin phosphorylase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQN55753.1	0.0	2	748	3	749
QQB62731.1	0.0	2	748	3	749
ACV28899.1	3.57e-236	2	742	7	743
QZO77069.1	6.38e-104	11	691	10	690
QUY64655.1	1.25e-103	11	691	10	690

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4Z5X_A	5.09e-64	10	751	30	825	Glycogenphosphorylase in complex with gallic acid [Oryctolagus cuniculus]
2GJ4_A	5.52e-64	10	751	18	813	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2FFR_A	5.59e-64	10	751	18	813	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
2GM9_A	5.59e-64	10	751	18	813	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]
1ABB_A	5.80e-64	10	751	20	815	ControlOf Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_B Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_C Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_D Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9XTL9	1.36e-69	8	751	28	825	Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
P39123	4.41e-68	22	751	22	791	Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
P79334	3.36e-65	10	751	30	825	Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
O18751	2.23e-64	10	751	30	825	Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
Q9CN90	4.23e-64	25	733	39	793	Glycogen phosphorylase OS=Pasteurella multocida (strain Pm70) OX=272843 GN=glgP PE=3 SV=1

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	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001424_00480.