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CAZyme Information: MGYG000000345_00573

You are here: Home > Sequence: MGYG000000345_00573

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species UBA1829 sp002338895
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1829; UBA1829 sp002338895
CAZyme ID MGYG000000345_00573
CAZy Family GT35
CAZyme Description Maltodextrin phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
826 MGYG000000345_2|CGC2 93543.03 6.3784
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000345 3773289 MAG Sweden Europe
Gene Location Start: 340112;  End: 342592  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 92 805 1.8e-281 0.9970326409495549

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14986 PRK14986 0.0 6 808 15 813
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 9 807 10 750
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 63 803 61 794
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 12 805 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 9 805 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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CEF63586.1 0.0 8 814 54 867
BBI18979.1 0.0 8 814 29 838
CEF63889.1 0.0 8 814 26 839
ABQ25900.1 0.0 7 819 17 830
ACH70729.1 0.0 8 817 28 841

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ZCP_A 0.0 8 817 28 840
Rabbitmuscle glycogen phosphorylase b in complex with N- cyclohexancarbonyl-N-beta-D-glucopyranosyl urea determined at 1.83 A resolution [Oryctolagus cuniculus]
3ZCS_A 0.0 8 817 28 840
Rabbitmuscle glycogen phosphorylase b in complex with N-(1-naphthoyl) -N-beta-D-glucopyranosyl urea determined at 2.07 A resolution [Oryctolagus cuniculus]
3ZCQ_A 0.0 8 817 28 840
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]
4EJ2_A 0.0 8 814 16 825
Crystalstructure of GPb in complex with DK10 [Oryctolagus cuniculus],4EKE_A Crystal structure of GPb in complex with DK11 [Oryctolagus cuniculus],4EKY_A Crystal structure of GPb in complex with DK15 [Oryctolagus cuniculus],4EL0_A Crystal structure of GPb in complex with DK16 [Oryctolagus cuniculus],4EL5_A Crystal structure of GPb in complex with DK12 [Oryctolagus cuniculus],4MHO_A Crystal structure of Gpb in complex with S3, SUGAR (N-[(BIPHENYL-4-YLOXY)ACETYL]-BETA-D-GLUCOPYRANOSYLAMINE) [Oryctolagus cuniculus],4MHS_A Crystal structure of Gpb in complex with SUGAR (N-[(2E)-3-(BIPHENYL-4-YL)PROP-2-ENOYL]-BETA-D-GLUCOPYRANOSYLAMINE [Oryctolagus cuniculus],4MI3_A Crystal structure of Gpb in complex with SUGAR (N-{(2R)-2-METHYL-3-[4-(PROPAN-2-YL)PHENYL]PROPANOYL}-BETA-D-GLUCOPYRANOSYLAMINE) (S21) [Oryctolagus cuniculus],4MI6_A Crystal structure of Gpb in complex with SUGAR (N-[4-(5,6,7,8-TETRAHYDRONAPHTHALEN-2-YL)BUTANOYL]-BETA-D-GLUCOPYRANOSYLAMINE) [Oryctolagus cuniculus],4MI9_A Crystal structure of Gpb in complex with SUGAR (N-[(3R)-3-(4-ETHYLPHENYL)BUTANOYL]-BETA-D-GLUCOPYRANOSYLAMINE) (S20) [Oryctolagus cuniculus],4MIC_A Crystal structure of Gpb in complex with SUGAR (N-{(2E)-3-[4-(PROPAN-2-YL)PHENYL]PROP-2-ENOYL}-BETA-D-GLUCOPYRANOSYLAMINE) (S6) [Oryctolagus cuniculus],4MRA_A Crystal structure of Gpb in complex with QUERCETIN [Oryctolagus cuniculus]
3NC4_A 0.0 8 817 26 838
Thebinding of beta-D-glucopyranosyl-thiosemicarbazone derivatives to glycogen phosphorylase: a new class of inhibitors [Oryctolagus cuniculus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P53534 0.0 8 813 28 836
Glycogen phosphorylase, brain form (Fragment) OS=Rattus norvegicus OX=10116 GN=Pygb PE=1 SV=3
Q5R5M6 0.0 8 813 28 836
Glycogen phosphorylase, brain form OS=Pongo abelii OX=9601 GN=PYGB PE=2 SV=3
P79334 0.0 8 817 28 840
Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
Q8CI94 0.0 8 813 28 836
Glycogen phosphorylase, brain form OS=Mus musculus OX=10090 GN=Pygb PE=1 SV=3
P11217 0.0 8 817 28 840
Glycogen phosphorylase, muscle form OS=Homo sapiens OX=9606 GN=PYGM PE=1 SV=6

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
1.000079 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000345_00573.