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CAZyme Information: MGYG000000014_01491
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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 | Clostridium butyricum | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium butyricum | |||||||||||
| CAZyme ID | MGYG000000014_01491 | |||||||||||
| CAZy Family | GT35 | |||||||||||
| CAZyme Description | Glycogen phosphorylase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 240846; End: 243209 Strand: + | |||||||||||
Full Sequence Download help
| MVDKEKIKNG IERYLKVKHG VKVKDAKDYE IFNAVSLTVL EEIIDNWNET SDTYNRGRMA | 60 |
| YYLSAEYLMG RALGNNLMNL GLYDNVKEVL CEMKIDINKI EEIEEDAGLG NGGLGRLAAC | 120 |
| FIESAATLNM PLMGYGIRYS NGLFKQNIEN GFQTECEDTW LKYGEAWSIR KDSETQIIKF | 180 |
| SDMTVKAVPY DVPIIGYGTK NINTLRLWQC EALREFDFNL FNNQQYIEAV SARNKAEDIS | 240 |
| RVLYPNDTAE AGKILRLRQQ YFFSSASMKD IIKKHKTKYG SDFSEFAKNN VAQLNDTHPT | 300 |
| ISILEFLRIL VDEENVDFTT ALGIAKEFFA YTNHTILAEA LEKWDIRLID RLFPRILQIA | 360 |
| YAVDDALMNE LRQKGYDEGA IWNFRIVAND VIRMANLAIF VGRAVNGVAA LHTEILKKHE | 420 |
| LNNWYNLYPN KFQNKTNGIT PRRWLRLCNS ELSEFITDLL GNEEWVKNLS LLKDLEKYMD | 480 |
| DEDVLERLMD IKHEKKIQLA AYIKQEEGII IDPDSFFDIQ IKRLHEYKRQ LLNALYILDL | 540 |
| YYRVKENPDL DIPKTTFIFG AKAFPGYRRA KGIVKFINEI ARLIDSDDQA SKKMKVVFVH | 600 |
| NYRVSYAQKL FPGSDLSKQI STAGKEASGT GNMKFMLNAT PTFGTYDGAN IEIVQASGEE | 660 |
| NNYIFGLRVE DIEKINHSYD PKAYYRDNPS IKRAVDTLIN GTLDDGGTGY FEDLYNALLE | 720 |
| ERDQYYLLAD FESFKKTEEM VFEDYRDKKK WAKKCLANLA NVGQFSSDRT IKQYADEIWD | 780 |
| IKPDAVR | 787 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT35 | 90 | 782 | 3.8e-257 | 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 | 26 | 783 | 36 | 812 | glycogen phosphorylase; Provisional |
| COG0058 | GlgP | 0.0 | 2 | 783 | 4 | 750 | Glucan phosphorylase [Carbohydrate transport and metabolism]. |
| PRK14985 | PRK14985 | 0.0 | 34 | 782 | 37 | 797 | maltodextrin phosphorylase; Provisional |
| TIGR02093 | P_ylase | 0.0 | 11 | 781 | 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 | 8 | 781 | 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 |
|---|---|---|---|---|---|
| QGH25606.1 | 0.0 | 1 | 787 | 1 | 787 |
| QGH21568.1 | 0.0 | 1 | 787 | 1 | 787 |
| QMW92028.1 | 0.0 | 1 | 787 | 1 | 787 |
| QJU45232.1 | 0.0 | 1 | 787 | 1 | 787 |
| BBK75733.1 | 0.0 | 1 | 787 | 1 | 787 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2C4M_A | 1.83e-262 | 26 | 783 | 28 | 790 | 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] |
| 5OX0_A | 9.17e-224 | 7 | 787 | 28 | 834 | GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus] |
| 2GJ4_A | 1.41e-223 | 7 | 787 | 16 | 822 | Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus] |
| 2GM9_A | 1.45e-223 | 7 | 787 | 16 | 822 | 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] |
| 2FFR_A | 1.45e-223 | 7 | 787 | 16 | 822 | Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P73511 | 5.24e-227 | 30 | 783 | 52 | 828 | Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1 |
| Q9XTL9 | 4.05e-225 | 7 | 783 | 28 | 830 | Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2 |
| P79334 | 2.43e-223 | 7 | 783 | 28 | 830 | Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3 |
| Q9WUB3 | 6.88e-223 | 7 | 787 | 28 | 834 | Glycogen phosphorylase, muscle form OS=Mus musculus OX=10090 GN=Pygm PE=1 SV=3 |
| O18751 | 9.73e-223 | 7 | 783 | 28 | 830 | Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 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 |
|---|---|---|---|---|---|
| 1.000090 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |