dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000004578_00256

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Basic Information help

Species

UMGS1795 sp900553555

Lineage

Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-552; UMGS1795; UMGS1795 sp900553555

CAZyme ID

MGYG000004578_00256

CAZy Family

GT35

CAZyme Description

Glycogen phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
807		91604.6	6.5536

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004578	1540237	MAG	France	Europe

Gene Location

Start: 50892; End: 53315 Strand: +

Full Sequence Download help

Enzyme Prediction help

EC	2.4.1.1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT35	94	800	2e-258	0.9955489614243324

CDD Domains download full data without filtering help

Cdd ID	Domain	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	35	802	44	813	glycogen phosphorylase; Provisional
COG0058	GlgP	2	801	3	750	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	25	800	27	797	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	12	799	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	9	799	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 help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANU55021.1	1.13e-314	3	802	5	800
ASB41745.1	1.13e-314	3	802	5	800
QQR31011.1	1.13e-314	3	802	5	800
CAB1239238.1	2.91e-314	8	802	10	800
BCI59382.1	1.72e-310	3	804	7	805

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2GJ4_A	1.35e-226	27	801	35	818	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A	1.39e-226	27	801	35	818	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]
7O8E_A	1.64e-226	27	801	40	823	ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]
1ABB_A	2.17e-226	27	801	37	820	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]
1C50_A	2.32e-226	27	801	34	817	IdentificationAnd Structural Characterization Of A Novel Allosteric Binding Site Of Glycogen Phosphorylase B [Oryctolagus cuniculus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39123	1.64e-250	7	802	3	797	Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
P73511	5.82e-248	3	802	24	829	Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
P45180	7.88e-233	2	805	16	820	Glycogen phosphorylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=glgP PE=3 SV=1
Q9CN90	2.29e-231	2	802	16	817	Glycogen phosphorylase OS=Pasteurella multocida (strain Pm70) OX=272843 GN=glgP PE=3 SV=1
P0AC86	5.89e-231	3	802	12	813	Glycogen phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=glgP PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000063	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000004578_00256.