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CAZyme Information: MGYG000002508_03787

You are here: Home > Sequence: MGYG000002508_03787

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 Hafnia alvei
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Hafnia; Hafnia alvei
CAZyme ID MGYG000002508_03787
CAZy Family GT35
CAZyme Description Maltodextrin phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
815 93351.79 6.1254
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002508 4498956 Isolate South Korea Asia
Gene Location Start: 4157404;  End: 4159851  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 101 811 1.8e-283 0.9985163204747775

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14986 PRK14986 0.0 1 815 1 815
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 9 812 1 750
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 38 811 31 797
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 21 810 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 18 810 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
AWV46524.1 0.0 1 815 1 815
AIU74594.1 0.0 1 815 1 815
QBJ34931.1 0.0 1 815 1 815
QIP57770.1 0.0 1 815 1 815
ANC40340.1 0.0 1 815 1 815

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5IKO_A 5.43e-292 14 811 28 832
Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
3ZCP_A 1.04e-288 11 811 22 829
Rabbitmuscle glycogen phosphorylase b in complex with N- cyclohexancarbonyl-N-beta-D-glucopyranosyl urea determined at 1.83 A resolution [Oryctolagus cuniculus]
2GJ4_A 1.09e-288 11 811 10 817
Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2FFR_A 1.13e-288 11 811 10 817
Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
2GM9_A 1.13e-288 11 811 10 817
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      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9CN90 0.0 3 814 8 818
Glycogen phosphorylase OS=Pasteurella multocida (strain Pm70) OX=272843 GN=glgP PE=3 SV=1
P45180 0.0 3 815 8 819
Glycogen phosphorylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=glgP PE=3 SV=1
P0AC87 0.0 1 815 1 815
Glycogen phosphorylase OS=Shigella flexneri OX=623 GN=glgP PE=3 SV=1
P0AC86 0.0 1 815 1 815
Glycogen phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=glgP PE=3 SV=1
P53534 9.80e-293 14 811 25 829
Glycogen phosphorylase, brain form (Fragment) OS=Rattus norvegicus OX=10116 GN=Pygb PE=1 SV=3

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
1.000060 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002508_03787.