CAZyme Information: MGYG000001812_02139

Basic Information

• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829
• CAZyme ID: MGYG000001812_02139
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
821	MGYG000001812_111|CGC1	93804.25	5.8306

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001812	3064175	MAG	Denmark	Europe

• Gene Location: Start: 5761; End: 8226 Strand: +

Full Sequence      

MPSSLKDQIKEAFIHHLTRSLAKRPEKASNLDRYHALALSIRDMMVERWIATKDEYEDKH
PRTVYYISLEFLMGRTLGNAMINLGVCEAATEAMKELGFNPDELFDEEVDAGLGNGGLGR
LAACFLDSMATLELPSYGYGIRYDYGIFKQIIQNGYQVEEPDNWLSRGNPWEVRRPELAR
VIQFGGRVEQHPDDRNPYRRKWVDTQEVLAMPYDTPIPGYRNNTVNTLRLWSAESLCGFN
LSKFNQGDYISANLEASMDQNITKVLYPNDNNYEGKELRLKQQYFLVSATLQDIIGRIKF
YGADMHDFAKESVIQLNDTHPALAIPELMRLLIDVENFSWDEAWKICTETFNYTNHTLMS
EALEKWPTALMEKLLPRHLEIIYEINFRFLRQVATKYIGDTERLGRMSLIQERPEKMVRM
AYMCVAVSHKVNGVATLHTELLKDGLFKDFNDFFPDKFVNITNGITPRRWLRKANPELSD
LITGRIGDNWVRNLDDLKALEAYANDREFLFNLAAVKRKNKLRLAKYIYENNGIAVNPDS
IFDVQVKRLHEYKRQLLNILHAITLYLEIKDNPDADFVPRTILFGAKAAPGYYMAKLIIK
LINAVSEVINEDPAVGDKLKIVFLSNYRVSLAEKIIPAADLSEQISLAGTEASGTGNMKF
ALNGALTIGTMDGANIEIHDAVGKDNIFIFGMNVEEVKALQARGYDPSEYIARNPLLKRA
LNLIKANFFSPAEIDVFRPIIDSFAYDTYMTAADFGSYAQVQKEVSGLYRNTEDWQRRAL
MNIANMGMFSSDRSIHEYATRIWDISPLPVSLESARGLELK

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	93	805	6.1e-282	0.9970326409495549

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	7	808	15	813	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	1	807	1	750	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	62	803	59	794	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	13	805	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	805	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
CEF63889.1	0.0	9	812	26	837
CCD70899.1	0.0	9	817	26	845
CCD70898.1	0.0	9	817	62	881
NP_504007.1	0.0	9	817	62	881
CEF63586.1	0.0	9	812	54	865

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2ZB2_A	0.0	8	814	29	841	Humanliver glycogen phosphorylase a complexed with glcose and 5-chloro-N-[4-(1,2-dihydroxyethyl)phenyl]-1H-indole-2-carboxamide [Homo sapiens],2ZB2_B Human liver glycogen phosphorylase a complexed with glcose and 5-chloro-N-[4-(1,2-dihydroxyethyl)phenyl]-1H-indole-2-carboxamide [Homo sapiens]
3ZCP_A	0.0	8	807	27	830	Rabbitmuscle glycogen phosphorylase b in complex with N- cyclohexancarbonyl-N-beta-D-glucopyranosyl urea determined at 1.83 A resolution [Oryctolagus cuniculus]
3NC4_A	0.0	8	807	25	828	Thebinding of beta-D-glucopyranosyl-thiosemicarbazone derivatives to glycogen phosphorylase: a new class of inhibitors [Oryctolagus cuniculus]
3DD1_A	0.0	8	814	28	840	Crystalstructure of glycogen phophorylase complexed with an anthranilimide based inhibitor GSK254 [Homo sapiens],3DD1_B Crystal structure of glycogen phophorylase complexed with an anthranilimide based inhibitor GSK254 [Homo sapiens],3DDS_A Crystal structure of glycogen phosphorylase complexed with an anthranilimide based inhibitor GSK261 [Homo sapiens],3DDS_B Crystal structure of glycogen phosphorylase complexed with an anthranilimide based inhibitor GSK261 [Homo sapiens],3DDW_A Crystal structure of glycogen phosphorylase complexed with an anthranilimide based inhibitor GSK055 [Homo sapiens],3DDW_B Crystal structure of glycogen phosphorylase complexed with an anthranilimide based inhibitor GSK055 [Homo sapiens]
3ZCQ_A	0.0	8	807	27	830	Rabbitmuscle glycogen phosphorylase b in complex with N-(4- trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution [Oryctolagus cuniculus],3ZCR_A Rabbit muscle glycogen phosphorylase b in complex with N-(4-tert- butyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2.07 A resolution [Oryctolagus cuniculus],3ZCT_A Rabbit muscle glycogen phosphorylase b in complex with N-(2-naphthoyl) -N-beta-D-glucopyranosyl urea determined at 2.0 A resolution [Oryctolagus cuniculus],3ZCU_A Rabbit muscle glycogen phosphorylase b in complex with N-(pyridyl-2- carbonyl)-N-beta-D-glucopyranosyl urea determined at 2.05 A resolution [Oryctolagus cuniculus],3ZCV_A Rabbit muscle glycogen phosphorylase b in complex with N-(indol-2- carbonyl)-N-beta-D-glucopyranosyl urea determined at 1.8 A resolution [Oryctolagus cuniculus],4CTM_A Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods [Oryctolagus cuniculus],4CTN_A Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods [Oryctolagus cuniculus],4CTO_A Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods [Oryctolagus cuniculus],4YI3_A Crystal structure of Gpb in complex with 4a [Oryctolagus cuniculus],4YI5_A Crystal structure of Gpb in complex with 4b [Oryctolagus cuniculus],4YUA_A Glycogen phosphorylase in complex with ellagic acid [Oryctolagus cuniculus],5JTT_A Crystal structure of GPb in complex with 8a [Oryctolagus cuniculus],5JTU_A Crystal structure of GPb in complex with 8b [Oryctolagus cuniculus],5LRD_A Crystal structure of Glycogen Phosphorylase b in complex with KS242 [Oryctolagus cuniculus],5MEM_A A potent fluorescent inhibitor of glycogen phosphorylase as a catalytic site probe. [Oryctolagus cuniculus],5O52_A Glycogen Phosphorylase b in complex with 33b [Oryctolagus cuniculus],5O54_A Glycogen Phosphorylase b in complex with 29a [Oryctolagus cuniculus],5O56_A Glycogen Phosphorylase b in complex with 29b [Oryctolagus cuniculus],5OWY_A Glycogen Phosphorylase in complex with KS252 [Oryctolagus cuniculus],5OWZ_A Glycogen Phosphorylase in complex with KS172 [Oryctolagus cuniculus],5OX1_A Glycogen Phosphorylase in complex with JLH270 [Oryctolagus cuniculus],5OX3_A Glycogen Phosphorylase in complex with SzB102v [Oryctolagus cuniculus],5OX4_A Glycogen Phosphorylase in complex with CK900 [Oryctolagus cuniculus],6F3J_A The crystal structure of Glycogen Phosphorylase in complex with 10a [Oryctolagus cuniculus],6F3L_A The crystal structure of Glycogen Phosphorylase in complex with 10b [Oryctolagus cuniculus],6F3R_A The crystal structure of Glycogen Phosphorylase in complex with 10c [Oryctolagus cuniculus],6F3S_A The crystal structure of Glycogen Phosphorylase in complex with 10d [Oryctolagus cuniculus],6F3U_A The crystal structure of Glycogen Phosphorylase in complex with 10h [Oryctolagus cuniculus],6QA6_A Glycogen Phosphorylase b in complex with 30 [Oryctolagus cuniculus],6QA7_A Glycogen Phosphorylase b in complex with 29 [Oryctolagus cuniculus],6QA8_A Glycogen Phosphorylase b in complex with 28 [Oryctolagus cuniculus],6R0H_A Glycogen Phosphorylase b in complex with 3 [Oryctolagus cuniculus],6R0I_A Glycogen Phosphorylase b in complex with 4 [Oryctolagus cuniculus],6S4H_A The crystal structure of glycogen phosphorylase in complex with 8 [Oryctolagus cuniculus],6S4K_A The crystal structure of glycogen phosphorylase in complex with 12 [Oryctolagus cuniculus],6S4O_A The crystal structure of glycogen phosphorylase in complex with 9 [Oryctolagus cuniculus],6S4P_A The crystal structure of glycogen phosphorylase in complex with 13 [Oryctolagus cuniculus],6S4R_A The crystal structure of glycogen phosphorylase in complex with 11 [Oryctolagus cuniculus],6S51_A The crystal structure of glycogen phosphorylase in complex with 10 [Oryctolagus cuniculus],6S52_A The crystal structure of glycogen phosphorylase in complex with 14 [Oryctolagus cuniculus],6YVE_AAA Chain AAA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q0VCM4	0.0	8	814	27	839	Glycogen phosphorylase, liver form OS=Bos taurus OX=9913 GN=PYGL PE=2 SV=1
Q5R5M6	0.0	8	807	27	830	Glycogen phosphorylase, brain form OS=Pongo abelii OX=9601 GN=PYGB PE=2 SV=3
Q5MIB5	0.0	8	812	27	835	Glycogen phosphorylase, liver form OS=Ovis aries OX=9940 GN=PYGL PE=2 SV=3
Q8CI94	0.0	8	807	27	830	Glycogen phosphorylase, brain form OS=Mus musculus OX=10090 GN=Pygb PE=1 SV=3
P79334	0.0	8	807	27	830	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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001812_02139.