You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000003010_00071
You are here: Home > Sequence: MGYG000003010_00071
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 | Granulicatella sp900551535 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; Granulicatella; Granulicatella sp900551535 | |||||||||||
| CAZyme ID | MGYG000003010_00071 | |||||||||||
| CAZy Family | GT35 | |||||||||||
| CAZyme Description | Glycogen phosphorylase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 16097; End: 18493 Strand: - | |||||||||||
Full Sequence Download help
| MVEKSLTSRV ETSLKNQFGV TISNASKRQV YEAMMRSVRD ILMEKKFSYE QTLKQTRQKR | 60 |
| AYYMSMEFLV GRTLRNNLFN LGIEKEAKEF LSENNFSLDE IYNMEPDPGL GNGGLGRLAA | 120 |
| CYLDALTSNE YPVTGFSILY EYGIFKQVIT NGWQQEFPDQ WLDLGKYGLV YRNDEEVEVR | 180 |
| FGGELEQVMT ETGLKVNHKN YTSIQAEPYD LLISGYDASA VNTLRLWEAK AKTGFNMKLF | 240 |
| ERGEYSKSSE AEAIASSISK LLYPADVTNE GKELRIKQQY FFISASLQQL VKNHYREFGT | 300 |
| LENFSEHVAL HINDTHPAMG VAELMRLLVD EYGYGWDKAW DITTKTFAYT NHTIMAEALE | 360 |
| KWPVSLFQPI LPRIYSIIEE INRRFCLWVM EQGKQYTLRD TAIIYDDMIK MANLSIVGSH | 420 |
| YVNGVSKLHS DILVRDTFKA FNDLYPGKFG NVTNGIAHRR WLGQANPELA TYLENLIGDD | 480 |
| FIKDLSGISK LNAYKDDEKV LKDLQAIKLT KKEQLATYIK ETLAISVNPH SIFDVQVKRL | 540 |
| HEYKRQLLNA LHIVYLYHEI KYNGLRPTPR TFIFAAKASS GYQMAKNIIK FIHSISQMIE | 600 |
| SDELVREYIK VVFIPDYKVT LAEIILPAAD VSEQISQAGK EASGTGNMKL MLNGAVTLGT | 660 |
| MDGANVEIYE AVGKDNIVIF GLETEEVDAL YAKGYKPWEY YNNSPKIKTV LDFIRTMTVG | 720 |
| GMNFNFIVDY LLTQDHYMCL ADFDSYVEAQ ERIEKDYNDS SKWMKMSLAN IANAGIFSAD | 780 |
| RAVKEYAKDI WHIKPVQG | 798 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT35 | 91 | 794 | 2.3e-260 | 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 | 25 | 797 | 36 | 814 | glycogen phosphorylase; Provisional |
| COG0058 | GlgP | 0.0 | 13 | 795 | 16 | 750 | Glucan phosphorylase [Carbohydrate transport and metabolism]. |
| PRK14985 | PRK14985 | 0.0 | 58 | 794 | 58 | 797 | maltodextrin phosphorylase; Provisional |
| TIGR02093 | P_ylase | 0.0 | 10 | 793 | 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 | 4 | 793 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QIX87764.1 | 0.0 | 1 | 797 | 1 | 797 |
| VEI38823.1 | 0.0 | 1 | 797 | 1 | 797 |
| QGS08182.1 | 0.0 | 1 | 797 | 1 | 797 |
| AXI27056.1 | 0.0 | 1 | 797 | 1 | 797 |
| AME09420.1 | 0.0 | 1 | 797 | 1 | 797 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3CEH_A | 6.62e-218 | 25 | 795 | 24 | 807 | 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] |
| 2GJ4_A | 1.52e-217 | 25 | 795 | 35 | 818 | Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus] |
| 2GM9_A | 1.56e-217 | 25 | 795 | 35 | 818 | 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 | 1.56e-217 | 25 | 795 | 35 | 818 | Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus] |
| 7O8E_A | 1.84e-217 | 25 | 795 | 40 | 823 | ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P39123 | 1.69e-234 | 19 | 796 | 21 | 797 | Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1 |
| P73511 | 2.89e-232 | 25 | 796 | 48 | 829 | Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1 |
| P45180 | 1.06e-230 | 25 | 797 | 41 | 818 | Glycogen phosphorylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=glgP PE=3 SV=1 |
| Q9CN90 | 3.95e-227 | 5 | 797 | 21 | 818 | Glycogen phosphorylase OS=Pasteurella multocida (strain Pm70) OX=272843 GN=glgP PE=3 SV=1 |
| P0AC86 | 5.75e-226 | 25 | 797 | 36 | 814 | Glycogen phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=glgP 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 |
|---|---|---|---|---|---|
| 1.000062 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |