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CAZyme Information: MGYG000001291_00290
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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 | Finegoldia magna_H | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Finegoldia; Finegoldia magna_H | |||||||||||
| CAZyme ID | MGYG000001291_00290 | |||||||||||
| CAZy Family | GT35 | |||||||||||
| CAZyme Description | Maltodextrin phosphorylase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 312623; End: 315001 Strand: + | |||||||||||
Full Sequence Download help
| MEKEEFLLRF EKILFNMFGK DLHTSTKKEK YIAFSKIIMN ELADDWKKTS DKHKHIRNAY | 60 |
| YFSAEFLIGR SLGNNLLNMG LDEKYSQILK ELDIDINDLE IQEEDAALGN GGLGRLAACF | 120 |
| MESAASLDYP LTGYGVRYRQ GLFKQYFHNG FQMEVGDNWT LDKDPWSRRV ESESKIIRYK | 180 |
| NQVVKAVPYD MPVVGYKNHV VNTLRLWQAE CDDGFDFQKF NNFQYDDSVK EKNRAEDITR | 240 |
| VLYPNDIQRP GKVLRLKQQY FFSSASIQDI IEKYEKNFPN DVNFEDFAKY NTIQLNDTHP | 300 |
| VMAIPEMMRV LMDDKKLSWK QAWNVTSNVF NYTNHTILQE AMEKWNVDVV EEVSPRIMDI | 360 |
| ITEIDRRFVS DLVGLYYSVD RIDNLRIVKD NTVNMAHLAI LTAVKINGVA KIHTEILKND | 420 |
| TLKPWHDLYP DKFVNKTNGI TPRRWLFYAN PELTQYITEL LGEDWKTDLT KLKELEKFRD | 480 |
| EDNVLDRLME IKLHNKIRLK KYIKEHEQID VDENSIFDIQ VKRLHEYKRQ LLNAFHILNL | 540 |
| YYKIKNNEIT DIPKQTYIFG AKAAPGYFRA KAIIKFINEV KNLVNNDDVV NKYIKVVFLE | 600 |
| NFNVSIGELV YPAADVSEQI STAGKEASGT GNMKFMLNGA LTVGTYDGAN IEIFNHAGED | 660 |
| NNFPFGATVD VLNSIRDNYN PVEYYYKDEN IKRVVDTLLS DLINDSGSFM FLDIYNSLVN | 720 |
| RDSSFKLDEY FVLKDFNDYE QIHEKILQTY ADKKKWAKMS LMNIANFGEF SSDRTIKEYA | 780 |
| EEIWRIVPNE KI | 792 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT35 | 89 | 786 | 3.5e-259 | 0.9955489614243324 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK14986 | PRK14986 | 0.0 | 12 | 788 | 24 | 812 | glycogen phosphorylase; Provisional |
| COG0058 | GlgP | 0.0 | 3 | 788 | 6 | 750 | Glucan phosphorylase [Carbohydrate transport and metabolism]. |
| PRK14985 | PRK14985 | 0.0 | 48 | 784 | 53 | 794 | maltodextrin phosphorylase; Provisional |
| TIGR02093 | P_ylase | 0.0 | 10 | 786 | 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 | 3 | 786 | 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 |
|---|---|---|---|---|---|
| BAG07682.1 | 0.0 | 1 | 792 | 1 | 792 |
| QKH79394.1 | 0.0 | 1 | 792 | 1 | 792 |
| QQK08557.1 | 0.0 | 1 | 786 | 1 | 786 |
| QQN56837.1 | 0.0 | 1 | 786 | 1 | 787 |
| QQB62166.1 | 0.0 | 1 | 786 | 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 | 3.44e-256 | 57 | 792 | 60 | 794 | 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] |
| 3CEH_A | 1.45e-223 | 57 | 790 | 58 | 809 | Humanliver glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE5688 [Homo sapiens],3CEH_B Human liver glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE5688 [Homo sapiens],3CEJ_A Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE2865 [Homo sapiens],3CEJ_B Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE2865 [Homo sapiens],3CEM_A Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE9423 [Homo sapiens],3CEM_B Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE9423 [Homo sapiens] |
| 1FA9_A | 4.79e-223 | 57 | 790 | 80 | 831 | HUMANLIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH AMP [Homo sapiens] |
| 1FC0_A | 4.79e-223 | 57 | 790 | 80 | 831 | HUMANLIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE [Homo sapiens],1FC0_B HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE [Homo sapiens],2ATI_A Glycogen Phosphorylase Inhibitors [Homo sapiens],2ATI_B Glycogen Phosphorylase Inhibitors [Homo sapiens] |
| 1XOI_A | 4.79e-223 | 57 | 790 | 80 | 831 | HumanLiver Glycogen Phosphorylase A complexed with Chloroindoloyl glycine amide [Homo sapiens],1XOI_B Human Liver Glycogen Phosphorylase A complexed with Chloroindoloyl glycine amide [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P73511 | 3.61e-223 | 57 | 788 | 82 | 828 | Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1 |
| P79334 | 1.63e-222 | 57 | 791 | 81 | 833 | Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3 |
| P06737 | 2.71e-222 | 57 | 790 | 81 | 832 | Glycogen phosphorylase, liver form OS=Homo sapiens OX=9606 GN=PYGL PE=1 SV=4 |
| O18751 | 4.61e-222 | 57 | 791 | 81 | 833 | Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3 |
| P09811 | 2.38e-221 | 57 | 790 | 81 | 832 | Glycogen phosphorylase, liver form OS=Rattus norvegicus OX=10116 GN=Pygl PE=1 SV=5 |
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 |
|---|---|---|---|---|---|
| 1.000050 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |