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CAZyme Information: MGYG000004740_01546
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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 | Eubacterium_I sp900557275 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_I; Eubacterium_I sp900557275 | |||||||||||
| CAZyme ID | MGYG000004740_01546 | |||||||||||
| CAZy Family | GT35 | |||||||||||
| CAZyme Description | Isoleucine--tRNA ligase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 4505; End: 10132 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT35 | 1148 | 1864 | 2.3e-281 | 0.9970326409495549 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PLN02882 | PLN02882 | 0.0 | 8 | 997 | 7 | 1019 | aminoacyl-tRNA ligase |
| pfam00133 | tRNA-synt_1 | 0.0 | 20 | 638 | 4 | 595 | tRNA synthetases class I (I, L, M and V). Other tRNA synthetase sub-families are too dissimilar to be included. |
| COG0058 | GlgP | 0.0 | 1078 | 1866 | 23 | 750 | Glucan phosphorylase [Carbohydrate transport and metabolism]. |
| cd04300 | GT35_Glycogen_Phosphorylase | 0.0 | 1066 | 1864 | 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. |
| PRK14986 | PRK14986 | 0.0 | 1083 | 1869 | 36 | 815 | glycogen phosphorylase; Provisional |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CBL11159.1 | 0.0 | 1054 | 1871 | 2 | 819 |
| VCV21023.1 | 0.0 | 1054 | 1871 | 2 | 819 |
| CBL07418.1 | 0.0 | 1055 | 1871 | 2 | 819 |
| BAK46498.1 | 0.0 | 1059 | 1874 | 12 | 828 |
| AEN95976.1 | 0.0 | 1056 | 1869 | 3 | 817 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1ILE_A | 4.81e-286 | 10 | 835 | 9 | 821 | Isoleucyl-TrnaSynthetase [Thermus thermophilus HB8],1JZQ_A Isoleucyl-tRNA synthetase Complexed with Isoleucyl-adenylate analogue [Thermus thermophilus],1JZS_A Isoleucyl-tRNA synthetase Complexed with mupirocin [Thermus thermophilus] |
| 5OX0_A | 4.62e-259 | 1036 | 1862 | 11 | 826 | GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus] |
| 7O8E_A | 8.24e-259 | 1036 | 1862 | 4 | 819 | ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus] |
| 1ABB_A | 1.08e-258 | 1036 | 1862 | 1 | 816 | 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] |
| 1AXR_A | 1.24e-258 | 1036 | 1862 | 10 | 825 | CooperativityBetween Hydrogen-Bonding And Charge-Dipole Interactions In The Inhibition Of Beta-Glycosidases By Azolopyridines: Evidence From A Study With Glycogen Phosphorylase B [Oryctolagus cuniculus],1E1Y_A Flavopiridol inhibits glycogen phosphorylase by binding at the inhibitor site [Oryctolagus cuniculus],1GPY_A CRYSTALLOGRAPHIC BINDING STUDIES ON THE ALLOSTERIC INHIBITOR GLUCOSE-6-PHOSPHATE TO T STATE GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],1PYG_A Structural Basis For The Activation Of Glycogen Phosphorylase B By Adenosine Monophosphate [Oryctolagus cuniculus],1PYG_B Structural Basis For The Activation Of Glycogen Phosphorylase B By Adenosine Monophosphate [Oryctolagus cuniculus],1PYG_C Structural Basis For The Activation Of Glycogen Phosphorylase B By Adenosine Monophosphate [Oryctolagus cuniculus],1PYG_D Structural Basis For The Activation Of Glycogen Phosphorylase B By Adenosine Monophosphate [Oryctolagus cuniculus],1UZU_A Glycogen Phosphorylase b in complex with indirubin-5'-sulphonate [Oryctolagus cuniculus],1XC7_A Binding of beta-D-glucopyranosyl bismethoxyphosphoramidate to glycogen phosphorylase b: Kinetic and crystallographic studies [Oryctolagus cuniculus],1XKX_A Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. [Oryctolagus cuniculus],1XL0_A Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. [Oryctolagus cuniculus],1XL1_A Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. [Oryctolagus cuniculus],1Z62_A Indirubin-3'-aminooxy-acetate inhibits glycogen phosphorylase by binding at the inhibitor and the allosteric site. Broad specificities of the two sites [Oryctolagus cuniculus],2AMV_A The Structure Of Glycogen Phosphorylase B With An Alkyl- Dihydropyridine-Dicarboxylic Acid [Oryctolagus cuniculus],2F3P_A Crystal Structure of the glycogen phosphorylase B / N-(beta-D-glucopyranosyl)oxamic acid complex [Oryctolagus cuniculus],2F3Q_A Crystal structure of the glycogen phosphorylase B / methyl-N-(beta-D-glucopyranosyl)oxamate complex [Oryctolagus cuniculus],2F3S_A Crystal Structure of the glycogen phosphorylase B / ethyl-N-(beta-D-glucopyranosyl)oxamate complex [Oryctolagus cuniculus],2F3U_A Crystal Structure of the glycogen phosphorylase B / N-(beta-D-glucopyranosyl)-N'-cyclopropyl oxalamide complex [Oryctolagus cuniculus],2FET_A Synthesis of C-D-Glycopyranosyl-Hydroquinones and-Benzoquinones. Inhibition of PTP1B. Inhibition of and binding to glycogen phosphorylase in the crystal [Oryctolagus cuniculus],2FF5_A Synthesis of C-D-Glycopyranosyl-Hydroquinones and-Benzoquinones. Inhibition of PTP1B. Inhibition of and binding to glycogen phosphorylase in the crystal [Oryctolagus cuniculus],3BD7_A Glycogen Phosphorylase complex with 1(-D-glucopyranosyl) thymine [Oryctolagus cuniculus],3BD8_A Glucogen Phosphorylase complex with 1(-D-glucopyranosyl) cytosine [Oryctolagus cuniculus],3BDA_A Glycogen Phosphorylase complex with 1(-D-glucopyranosyl) cyanuric acid [Oryctolagus cuniculus],5LRC_A Crystal structure of Glycogen Phosphorylase in complex with KS114 [Oryctolagus cuniculus],5LRE_A Crystal structure of Glycogen Phosphorylase b in complex with KS382 [Oryctolagus cuniculus],5LRF_A Crystal structure of Glycogen Phosphorylase b in complex with KS389 [Oryctolagus cuniculus],5O50_A Glycogen Phosphorylase b in complex with 33a [Oryctolagus cuniculus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q6HJF2 | 0.0 | 4 | 1048 | 3 | 1027 | Isoleucine--tRNA ligase 2 OS=Bacillus thuringiensis subsp. konkukian (strain 97-27) OX=281309 GN=ileS2 PE=3 SV=1 |
| Q81E30 | 0.0 | 4 | 1041 | 3 | 1020 | Isoleucine--tRNA ligase 2 OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=ileS2 PE=3 SV=2 |
| Q739A1 | 0.0 | 4 | 1048 | 3 | 1027 | Isoleucine--tRNA ligase 2 OS=Bacillus cereus (strain ATCC 10987 / NRS 248) OX=222523 GN=ileS2 PE=3 SV=1 |
| Q81R75 | 0.0 | 4 | 1048 | 3 | 1027 | Isoleucine--tRNA ligase 2 OS=Bacillus anthracis OX=1392 GN=ileS2 PE=3 SV=1 |
| Q63BZ8 | 0.0 | 4 | 1048 | 3 | 1027 | Isoleucine--tRNA ligase 2 OS=Bacillus cereus (strain ZK / E33L) OX=288681 GN=ileS2 PE=3 SV=1 |
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 |
|---|---|---|---|---|---|
| 1.000046 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |