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CAZyme Information: MGYG000000839_00810
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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 | Clostridium sp900540255 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900540255 | |||||||||||
| CAZyme ID | MGYG000000839_00810 | |||||||||||
| CAZy Family | GH130 | |||||||||||
| CAZyme Description | 4-O-beta-D-mannosyl-D-glucose phosphorylase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 228; End: 1406 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH130 | 58 | 360 | 7.6e-83 | 0.9594594594594594 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd08993 | GH130 | 1.12e-95 | 66 | 357 | 2 | 279 | Glycosyl hydrolase family 130. This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), among others that have yet to be characterized. They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor. This family includes Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) and beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2), enzymes that phosphorolyze beta-mannosidic linkages at the non-reducing ends of their substrates, and have substantially diverse substrate specificity that are determined by three loop regions. |
| cd18607 | GH130 | 9.17e-75 | 66 | 350 | 2 | 268 | Glycoside hydrolase family 130. Members of the glycosyl hydrolase family 130, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor. |
| cd18615 | GH130 | 1.32e-36 | 67 | 351 | 5 | 277 | Glycosyl hydrolase family 130; uncharacterized. This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor. |
| cd18614 | GH130 | 5.24e-31 | 68 | 350 | 4 | 273 | Glycosyl hydrolase family 130; uncharacterized. This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor. |
| COG2152 | COG2152 | 1.28e-29 | 53 | 359 | 14 | 308 | Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QNF27010.1 | 5.45e-226 | 1 | 389 | 1 | 390 |
| BAM48377.1 | 2.58e-224 | 1 | 392 | 1 | 393 |
| AML27056.1 | 1.78e-219 | 1 | 391 | 1 | 391 |
| QOS81689.1 | 2.82e-219 | 1 | 388 | 1 | 389 |
| QLG37878.1 | 2.31e-218 | 1 | 391 | 1 | 392 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5AY9_A | 1.80e-172 | 1 | 388 | 1 | 386 | Crystalstructure of Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) [Ruminococcus albus 7 = DSM 20455],5AYC_A Crystal structure of Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) in complexes with sulfate and 4-O-beta-D-mannosyl-D-glucose [Ruminococcus albus 7 = DSM 20455] |
| 3WAS_A | 4.80e-159 | 1 | 389 | 3 | 390 | Crystalstructure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with Man-Glc+PO4 [Bacteroides fragilis NCTC 9343],3WAS_B Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with Man-Glc+PO4 [Bacteroides fragilis NCTC 9343],3WAT_A Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with Man+Glc [Bacteroides fragilis NCTC 9343],3WAT_B Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with Man+Glc [Bacteroides fragilis NCTC 9343],3WAU_A Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with M1P [Bacteroides fragilis NCTC 9343],3WAU_B Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with M1P [Bacteroides fragilis NCTC 9343],4KMI_A Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with PO4 [Bacteroides fragilis NCTC 9343],4KMI_B Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with PO4 [Bacteroides fragilis NCTC 9343] |
| 1VKD_A | 3.12e-27 | 72 | 359 | 58 | 332 | Crystalstructure of a predicted glycosidase (tm1225) from thermotoga maritima msb8 at 2.10 A resolution [Thermotoga maritima MSB8],1VKD_B Crystal structure of a predicted glycosidase (tm1225) from thermotoga maritima msb8 at 2.10 A resolution [Thermotoga maritima MSB8],1VKD_C Crystal structure of a predicted glycosidase (tm1225) from thermotoga maritima msb8 at 2.10 A resolution [Thermotoga maritima MSB8],1VKD_D Crystal structure of a predicted glycosidase (tm1225) from thermotoga maritima msb8 at 2.10 A resolution [Thermotoga maritima MSB8],1VKD_E Crystal structure of a predicted glycosidase (tm1225) from thermotoga maritima msb8 at 2.10 A resolution [Thermotoga maritima MSB8],1VKD_F Crystal structure of a predicted glycosidase (tm1225) from thermotoga maritima msb8 at 2.10 A resolution [Thermotoga maritima MSB8] |
| 5AYD_A | 2.40e-17 | 166 | 359 | 140 | 328 | Crystalstructure of Ruminococcus albus beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) in complexes with phosphate [Ruminococcus albus 7 = DSM 20455],5AYD_B Crystal structure of Ruminococcus albus beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) in complexes with phosphate [Ruminococcus albus 7 = DSM 20455],5AYD_C Crystal structure of Ruminococcus albus beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) in complexes with phosphate [Ruminococcus albus 7 = DSM 20455],5AYD_D Crystal structure of Ruminococcus albus beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) in complexes with phosphate [Ruminococcus albus 7 = DSM 20455],5AYD_E Crystal structure of Ruminococcus albus beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) in complexes with phosphate [Ruminococcus albus 7 = DSM 20455],5AYD_F Crystal structure of Ruminococcus albus beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) in complexes with phosphate [Ruminococcus albus 7 = DSM 20455],5AYE_A Crystal structure of Ruminococcus albus beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) in complexes with phosphate and beta-(1,4)-mannobiose [Ruminococcus albus 7 = DSM 20455],5AYE_B Crystal structure of Ruminococcus albus beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) in complexes with phosphate and beta-(1,4)-mannobiose [Ruminococcus albus 7 = DSM 20455],5AYE_C Crystal structure of Ruminococcus albus beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) in complexes with phosphate and beta-(1,4)-mannobiose [Ruminococcus albus 7 = DSM 20455],5AYE_D Crystal structure of Ruminococcus albus beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) in complexes with phosphate and beta-(1,4)-mannobiose [Ruminococcus albus 7 = DSM 20455],5AYE_E Crystal structure of Ruminococcus albus beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) in complexes with phosphate and beta-(1,4)-mannobiose [Ruminococcus albus 7 = DSM 20455],5AYE_F Crystal structure of Ruminococcus albus beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) in complexes with phosphate and beta-(1,4)-mannobiose [Ruminococcus albus 7 = DSM 20455] |
| 7FIP_A | 1.32e-15 | 69 | 356 | 36 | 311 | ChainA, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIP_B Chain B, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIP_C Chain C, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIP_D Chain D, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIQ_A Chain A, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIQ_B Chain B, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIQ_C Chain C, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIQ_D Chain D, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIR_A Chain A, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIR_B Chain B, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIR_C Chain C, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIR_D Chain D, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIS_A Chain A, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIS_B Chain B, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIS_C Chain C, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514],7FIS_D Chain D, Beta-1,2-mannobiose phosphorylase [Thermoanaerobacter sp. X514] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| E6UIS7 | 9.86e-172 | 1 | 388 | 1 | 386 | 4-O-beta-D-mannosyl-D-glucose phosphorylase OS=Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7) OX=697329 GN=Rumal_0852 PE=1 SV=1 |
| Q5LH68 | 2.63e-158 | 1 | 389 | 3 | 390 | 4-O-beta-D-mannosyl-D-glucose phosphorylase OS=Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow) OX=272559 GN=BF0772 PE=1 SV=1 |
| E6UBR9 | 1.31e-16 | 166 | 359 | 140 | 328 | Beta-1,4-mannooligosaccharide phosphorylase OS=Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7) OX=697329 GN=Rumal_0099 PE=1 SV=1 |
| B0K2C3 | 6.40e-15 | 69 | 356 | 25 | 300 | Beta-1,2-mannobiose phosphorylase OS=Thermoanaerobacter sp. (strain X514) OX=399726 GN=Teth514_1789 PE=1 SV=1 |
| Q8A8Y4 | 1.18e-13 | 187 | 363 | 144 | 319 | 1,4-beta-mannosyl-N-acetylglucosamine phosphorylase OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=BT_1033 PE=1 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 |
|---|---|---|---|---|---|
| 1.000045 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |