dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; UMGS1004;

CAZyme ID

MGYG000002790_01099

CAZy Family

GT35

CAZyme Description

Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
595		67699.89	5.8561

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002790	1254341	MAG	United States	North America

Gene Location

Start: 546; End: 2333 Strand: -

Enzyme Prediction help

EC	2.4.1.1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT35	6	594	2.6e-205	0.8471810089020771

CDD Domains download full data without filtering help

Cdd ID	Domain	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	10	595	211	811	glycogen phosphorylase; Provisional
COG0058	GlgP	12	594	178	748	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	7	592	197	794	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	8	594	193	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	7	594	195	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
CUH92218.1	5.07e-223	3	593	171	778
ADU23251.1	8.87e-221	3	594	176	787
ADU28082.1	2.29e-219	3	592	170	775
AYF39756.1	2.29e-219	3	592	170	775
AVQ97094.1	2.29e-219	3	592	170	775

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C4M_A	4.17e-187	1	594	178	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	1.04e-161	3	592	217	829	Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
1L5V_A	5.55e-161	9	592	196	792	CrystalStructure of the Maltodextrin Phosphorylase complexed with Glucose-1-phosphate [Escherichia coli],1L5V_B Crystal Structure of the Maltodextrin Phosphorylase complexed with Glucose-1-phosphate [Escherichia coli],1L5W_A Crystal Structure of the Maltodextrin Phosphorylase Complexed with the Products of the Enzymatic Reaction between Glucose-1-phosphate and Maltotetraose [Escherichia coli],1L5W_B Crystal Structure of the Maltodextrin Phosphorylase Complexed with the Products of the Enzymatic Reaction between Glucose-1-phosphate and Maltotetraose [Escherichia coli],1L6I_A Crystal Structure of the Maltodextrin Phosphorylase complexed with the products of the enzymatic reaction between glucose-1-phosphate and maltopentaose [Escherichia coli],1L6I_B Crystal Structure of the Maltodextrin Phosphorylase complexed with the products of the enzymatic reaction between glucose-1-phosphate and maltopentaose [Escherichia coli],2ASV_A Chain A, Maltodextrin phosphorylase [Escherichia coli],2ASV_B Chain B, Maltodextrin phosphorylase [Escherichia coli],2AV6_A Chain A, Maltodextrin phosphorylase [Escherichia coli],2AV6_B Chain B, Maltodextrin phosphorylase [Escherichia coli],2AW3_A X-Ray studies on maltodextrin phosphorylase complexes: recognition of substrates and cathalitic mechanism of phosphorylase family [Escherichia coli],2AW3_B X-Ray studies on maltodextrin phosphorylase complexes: recognition of substrates and cathalitic mechanism of phosphorylase family [Escherichia coli],2AZD_A Chain A, Maltodextrin phosphorylase [Escherichia coli],2AZD_B Chain B, Maltodextrin phosphorylase [Escherichia coli]
1E4O_A	7.84e-161	9	592	196	792	Phosphorylaserecognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli],1E4O_B Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli],1QM5_A Phosphorylase recognition and phosphorylysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli],1QM5_B Phosphorylase recognition and phosphorylysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli]
3CEH_A	9.01e-160	8	594	197	805	Humanliver glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE5688 [Homo sapiens],3CEH_B Human liver glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE5688 [Homo sapiens],3CEJ_A Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE2865 [Homo sapiens],3CEJ_B Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE2865 [Homo sapiens],3CEM_A Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE9423 [Homo sapiens],3CEM_B Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE9423 [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9PKE6	8.94e-164	7	595	209	810	Glycogen phosphorylase OS=Chlamydia muridarum (strain MoPn / Nigg) OX=243161 GN=glgP PE=3 SV=1
Q3B7M9	1.18e-162	3	592	214	826	Glycogen phosphorylase, brain form OS=Bos taurus OX=9913 GN=PYGB PE=2 SV=3
O84250	3.23e-161	7	595	209	810	Glycogen phosphorylase OS=Chlamydia trachomatis (strain D/UW-3/Cx) OX=272561 GN=glgP PE=3 SV=1
P73511	4.38e-161	6	592	224	824	Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
P11216	5.22e-161	3	592	214	826	Glycogen phosphorylase, brain form OS=Homo sapiens OX=9606 GN=PYGB PE=1 SV=5

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
1.000056	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000002790_01099.

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