Species | Kluyvera ascorbata_B | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Kluyvera; Kluyvera ascorbata_B | |||||||||||
CAZyme ID | MGYG000002491_04556 | |||||||||||
CAZy Family | GT35 | |||||||||||
CAZyme Description | Maltodextrin phosphorylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 22863; End: 25310 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT35 | 101 | 810 | 1.9e-282 | 0.9970326409495549 |
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 | 39 | 808 | 32 | 794 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QJO48475.1 | 0.0 | 1 | 815 | 1 | 815 |
QQM80240.1 | 0.0 | 1 | 815 | 1 | 815 |
ATR13155.1 | 0.0 | 1 | 815 | 1 | 815 |
BBS24740.1 | 0.0 | 1 | 815 | 1 | 815 |
AKL33002.1 | 0.0 | 1 | 815 | 1 | 815 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3ZCP_A | 2.97e-288 | 25 | 814 | 36 | 832 | Rabbitmuscle glycogen phosphorylase b in complex with N- cyclohexancarbonyl-N-beta-D-glucopyranosyl urea determined at 1.83 A resolution [Oryctolagus cuniculus] |
2GJ4_A | 3.10e-288 | 25 | 814 | 24 | 820 | Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus] |
2GM9_A | 3.21e-288 | 25 | 814 | 24 | 820 | 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] |
7O8E_A | 3.81e-288 | 25 | 814 | 29 | 825 | ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus] |
1ABB_A | 5.04e-288 | 25 | 814 | 26 | 822 | ControlOf 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9CN90 | 0.0 | 7 | 810 | 12 | 814 | Glycogen phosphorylase OS=Pasteurella multocida (strain Pm70) OX=272843 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 |
P0AC87 | 0.0 | 1 | 815 | 1 | 815 | Glycogen phosphorylase OS=Shigella flexneri OX=623 GN=glgP PE=3 SV=1 |
P45180 | 0.0 | 7 | 815 | 12 | 819 | Glycogen phosphorylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=glgP PE=3 SV=1 |
Q3B7M9 | 7.07e-289 | 25 | 808 | 36 | 826 | Glycogen phosphorylase, brain form OS=Bos taurus OX=9913 GN=PYGB PE=2 SV=3 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000083 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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