Species | Peptostreptococcus sp000758885 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Peptostreptococcus; Peptostreptococcus sp000758885 | |||||||||||
CAZyme ID | MGYG000003729_00108 | |||||||||||
CAZy Family | GT35 | |||||||||||
CAZyme Description | Glycogen phosphorylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2372; End: 4756 Strand: - |
MNHMTKDIEQ YLQTKFGNSL GESNERQLYQ ALMAETRNRL SKKRYDYTKK LKESGQKQAY | 60 |
YMSMEFLVGR TLRNNLFNLG IEGEVRSFLA EKNFDLDRIY DMEPDPGLGN GGLGRLASCY | 120 |
LDALTSNDYP VTGFSILYEF GIFKQVIANG WQQEYPDNWL GMGQYGLVHR SDEEIEVRFY | 180 |
GKTKEHWTNE GLKVSYEDYT SIIAEPYDLM ISGYKSEAVN VLRLWKSKAN AGFDMKLFER | 240 |
GEYARSSESE AIAESISKLL YPADDNDKGK ALRIKQQYFF TSASLQQIVK NHYKEYGTLD | 300 |
NLADKAAIHI NDTHPSMCIP ELMRILMDDY DYSWENAWDI TTKVFAYTNH TIMAEALEKW | 360 |
SVDLFAPILP RIYTIIREIN NRFCQYCNEI GAASDLESMS IIHNNMIRMA NLCIVGSYNV | 420 |
NGVSGLHTDI LKADTFEPFN RIYPGKFNNV TNGIAHRRWL GQANPELTGY LNGLLGGDFI | 480 |
KDLSNIEELL KYADDKTVLA DLEKIKRTKK EQLAKYIKDA NGINVDIDSI FDVQVKRLHE | 540 |
YKRQLLNALH IVYLYRQIKF NGLKPRPRTF IFAAKASSGY VMAKNIIKFI CTLSEMIESD | 600 |
PELRDYIKVV FLEDYRVTLA EIIIPGANVS EQISQAGKEA SGTGNMKLML NGALTLGTLD | 660 |
GANVEIHDAV GDENMFLFGL KTPEVNDLYA KGYRPRDYYE NVPAIKETLD FMRTINIDGT | 720 |
GFGNIVDYLI NHDPYMCLAD FESYVNKQAE VAEAYGDKDR WNKMSLVNIA KAGIFSADRA | 780 |
TQEYTDGIWH IDRV | 794 |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT35 | 89 | 791 | 2.2e-259 | 0.9955489614243324 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK14986 | PRK14986 | 0.0 | 57 | 794 | 70 | 813 | glycogen phosphorylase; Provisional |
COG0058 | GlgP | 0.0 | 7 | 793 | 12 | 750 | Glucan phosphorylase [Carbohydrate transport and metabolism]. |
PRK14985 | PRK14985 | 0.0 | 15 | 793 | 20 | 798 | maltodextrin phosphorylase; Provisional |
TIGR02093 | P_ylase | 0.0 | 8 | 791 | 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 | 6 | 791 | 2 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
VEI38823.1 | 0.0 | 8 | 794 | 10 | 796 |
QIX87764.1 | 0.0 | 8 | 794 | 10 | 796 |
QGS08182.1 | 0.0 | 8 | 794 | 10 | 796 |
SQH55554.1 | 0.0 | 8 | 794 | 10 | 796 |
AXI27056.1 | 0.0 | 8 | 794 | 10 | 796 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2GJ4_A | 2.16e-213 | 53 | 792 | 65 | 817 | Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus] |
2GM9_A | 2.23e-213 | 53 | 792 | 65 | 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] |
2FFR_A | 2.23e-213 | 53 | 792 | 65 | 817 | Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus] |
7TM7_A | 2.28e-213 | 55 | 793 | 66 | 804 | ChainA, Alpha-1,4 glucan phosphorylase [Klebsiella pneumoniae subsp. pneumoniae HS11286],7TM7_B Chain B, Alpha-1,4 glucan phosphorylase [Klebsiella pneumoniae subsp. pneumoniae HS11286] |
7O8E_A | 2.61e-213 | 53 | 792 | 70 | 822 | ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P73511 | 6.03e-225 | 11 | 794 | 39 | 829 | Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1 |
P39123 | 1.31e-224 | 12 | 791 | 16 | 794 | Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1 |
P0AC87 | 5.30e-220 | 57 | 794 | 70 | 813 | Glycogen phosphorylase OS=Shigella flexneri OX=623 GN=glgP PE=3 SV=1 |
P0AC86 | 5.30e-220 | 57 | 794 | 70 | 813 | Glycogen phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=glgP PE=3 SV=1 |
O84250 | 1.86e-217 | 57 | 793 | 66 | 811 | Glycogen phosphorylase OS=Chlamydia trachomatis (strain D/UW-3/Cx) OX=272561 GN=glgP PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000034 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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