CAZyme Information: MGYG000001650_00770

Basic Information

• Species: F23-B02 sp900760205
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; F23-B02; F23-B02 sp900760205
• CAZyme ID: MGYG000001650_00770
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
802		89921.55	5.9498

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001650	1589868	MAG	United States	North America

• Gene Location: Start: 895; End: 3303 Strand: -

Full Sequence      

MFTSQISRDEVRSAIEDKLCAHFAVTSKNASDDQVFQASAIVIREIMSRLLAAEETKKPG
REVHYLSMEFLMGRSLMKNAFNLGISEALTGALEDLGRNAADIFESENDAGLGNGGLGRL
AACYMDSLASLGIAATGYSICYELGIFRQKIADGKQTEVADDWRSAAESWLVARNDEAVE
IRFGGHIAPHWDSLGRYHAEHIGYQTVTAVPRDMLIAGYGGNEINTLRLWDARSTSALDM
YLFSEGEYVRSLEQRTMSEVITKVLYPADDHIEGKTLRLKQQYFFVSATTQCIVRKHMER
YGDIRSFAEHHVIQINDTHPTLVIPELMRIMMDEYGLGWDEAWRIVTASVAYTNHTVMSE
ALEKWPQELIQTLLPRVWEILCEINRRWCDYLVSKFGSSEKVGRNLIIKDGQVHMANLCL
AACYKINGVSGLHGRILKTELFKDICELGPERFTYVTNGIDHRRWLAQINPRLHALVSEL
LGGEGYLCRPEELSRLAGFAGDGAVRERANEIKRLNKCDFAAFLKRNDNFTLNTDAILDV
QVKRLHEYKRQLLCAMLITRLQMRLHDDPNMDFTPRSFVFGAKAAAGYRTAKRIIELICS
LAGDINNDPLCRGRLQVCFMENYRVSAAEALMPAAQVSEQISTAGKEASGTGNMKLMLNG
AVTIGTLDGANVEMYERLGDKNMFLFGLRAEEIDPLRASGYDPQRCAQADPELAAVLDRF
SKGFADGKSYSDLVSNLLYNGDPYMLCADFRDYVSTHDRLYSAISDPGERARLSIMNTAE
AGVFAADRAVREYAEGIWKIKL

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	92	801	4e-239	0.9985163204747775

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	61	801	70	811	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	3	801	1	749	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	34	801	33	797	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	15	800	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	12	800	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
QBB67026.1	1.01e-311	7	800	6	807
ALP95317.1	1.01e-311	7	800	6	807
ANU40324.1	1.12e-311	7	800	8	809
QQR06906.1	1.12e-311	7	800	8	809
QIA32151.1	1.43e-311	7	800	5	806

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2FFR_A	1.05e-210	33	801	39	817	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
1Z8D_A	1.79e-210	33	801	51	829	ChainA, Glycogen phosphorylase, muscle form [Homo sapiens]
3ZCP_A	1.85e-210	33	801	51	829	Rabbitmuscle glycogen phosphorylase b in complex with N- cyclohexancarbonyl-N-beta-D-glucopyranosyl urea determined at 1.83 A resolution [Oryctolagus cuniculus]
2GJ4_A	2.02e-210	33	801	39	817	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A	2.09e-210	33	801	39	817	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P73511	5.43e-211	6	801	24	827	Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
P11217	1.23e-210	33	801	51	829	Glycogen phosphorylase, muscle form OS=Homo sapiens OX=9606 GN=PYGM PE=1 SV=6
Q9Z8N1	1.96e-210	4	800	10	814	Glycogen phosphorylase OS=Chlamydia pneumoniae OX=83558 GN=glgP PE=3 SV=1
P00489	2.02e-209	33	801	51	829	Glycogen phosphorylase, muscle form OS=Oryctolagus cuniculus OX=9986 GN=PYGM PE=1 SV=3
P79334	2.77e-209	22	801	37	829	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
1.000054	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001650_00770.