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CAZyme Information: QHS65814.1

You are here: Home > Sequence: QHS65814.1

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 [Candida] glabrata
Lineage Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; [Candida] glabrata
CAZyme ID QHS65814.1
CAZy Family GH47
CAZyme Description Alpha-1,4 glucan phosphorylase [Source:UniProtKB/TrEMBL;Acc:A0A0W0CTB6]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
899 103082.79 5.2626
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CglabrataCBS1382020 5508 N/A 250 5258
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1:158

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 160 894 1.2e-271 0.9970326409495549

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
273967 P_ylase 0.0 71 893 1 793
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]
340853 GT35_Glycogen_Phosphorylase 0.0 68 893 1 794
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.
395272 Phosphorylase 0.0 161 894 1 661
Carbohydrate phosphorylase. The members of this family catalyze the formation of glucose 1-phosphate from one of the following polyglucoses; glycogen, starch, glucan or maltodextrin.
184948 PRK14986 0.0 94 898 44 814
glycogen phosphorylase; Provisional
223136 GlgP 0.0 63 896 5 750
Glucan phosphorylase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 899 1 899
0.0 1 899 1 899
0.0 1 899 1 899
0.0 1 899 1 899
0.0 1 899 1 899

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 24 897 1 878
Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. [Saccharomyces cerevisiae],1YGP_B Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. [Saccharomyces cerevisiae]
2.59e-265 62 896 11 818
Structure of rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2.68e-265 62 896 11 818
Structure of 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]
2.68e-265 62 896 11 818
Crystallographic studies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
4.20e-265 62 896 13 820
Control Of 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 1 897 1 901
Glycogen phosphorylase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GPH1 PE=1 SV=4
8.33e-297 28 896 12 842
Glycogen phosphorylase 1 OS=Dictyostelium discoideum OX=44689 GN=glpV PE=1 SV=3
2.28e-282 62 898 109 911
Glycogen phosphorylase 2 OS=Dictyostelium discoideum OX=44689 GN=glpD PE=1 SV=2
9.67e-270 92 896 53 830
Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
1.89e-266 62 896 23 830
Glycogen phosphorylase, muscle form OS=Mus musculus OX=10090 GN=Pygm PE=1 SV=3

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000061 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in QHS65814.1.