logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004560_01693

You are here: Home > Sequence: MGYG000004560_01693

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
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA737;
CAZyme ID MGYG000004560_01693
CAZy Family GH130
CAZyme Description 4-O-beta-D-mannosyl-D-glucose phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
398 MGYG000004560_20|CGC1 44773.63 6.3115
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004560 2385116 MAG France Europe
Gene Location Start: 18987;  End: 20183  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.281

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH130 51 361 6.8e-86 0.9898648648648649

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08993 GH130 4.29e-100 68 357 2 278
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 5.18e-77 68 350 2 267
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 4.26e-41 69 350 5 275
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 6.14e-37 46 362 1 310
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism].
cd18614 GH130 4.38e-36 70 350 4 272
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL34989.1 6.45e-219 4 389 3 389
CBK96123.1 1.06e-217 4 389 3 389
CCO04533.1 1.51e-217 5 389 4 389
BCJ97190.1 2.51e-215 15 390 11 387
BCJ96775.1 3.50e-214 15 394 11 391

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5AY9_A 3.56e-195 15 389 12 386
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 5.08e-165 4 390 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 1.38e-28 49 361 35 333
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 8.23e-23 51 361 28 329
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]
4UDG_A 8.50e-18 70 364 60 344
Crystalstructure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with N-acetylglucosamine and inorganic phosphate [uncultured organism],4UDG_B Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with N-acetylglucosamine and inorganic phosphate [uncultured organism],4UDG_C Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with N-acetylglucosamine and inorganic phosphate [uncultured organism],4UDG_D Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with N-acetylglucosamine and inorganic phosphate [uncultured organism],4UDG_E Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with N-acetylglucosamine and inorganic phosphate [uncultured organism],4UDG_F Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with N-acetylglucosamine and inorganic phosphate [uncultured organism],4UDI_A Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.85 Angstrom from unknown human gut bacteria (Uhgb_MP) [uncultured organism],4UDI_B Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.85 Angstrom from unknown human gut bacteria (Uhgb_MP) [uncultured organism],4UDI_C Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.85 Angstrom from unknown human gut bacteria (Uhgb_MP) [uncultured organism],4UDI_D Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.85 Angstrom from unknown human gut bacteria (Uhgb_MP) [uncultured organism],4UDI_E Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.85 Angstrom from unknown human gut bacteria (Uhgb_MP) [uncultured organism],4UDI_F Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.85 Angstrom from unknown human gut bacteria (Uhgb_MP) [uncultured organism],4UDJ_A Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with beta-D-mannopyranose and inorganic phosphate [uncultured organism],4UDJ_B Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with beta-D-mannopyranose and inorganic phosphate [uncultured organism],4UDJ_C Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with beta-D-mannopyranose and inorganic phosphate [uncultured organism],4UDJ_D Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with beta-D-mannopyranose and inorganic phosphate [uncultured organism],4UDJ_E Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with beta-D-mannopyranose and inorganic phosphate [uncultured organism],4UDJ_F Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with beta-D-mannopyranose and inorganic phosphate [uncultured organism],4UDK_A Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.76 Angstrom from unknown human gut bacteria (Uhgb_MP) in complex with N-acetyl-D-glucosamine, beta-D-mannopyranose and inorganic phosphate [uncultured organism],4UDK_B Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.76 Angstrom from unknown human gut bacteria (Uhgb_MP) in complex with N-acetyl-D-glucosamine, beta-D-mannopyranose and inorganic phosphate [uncultured organism],4UDK_C Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.76 Angstrom from unknown human gut bacteria (Uhgb_MP) in complex with N-acetyl-D-glucosamine, beta-D-mannopyranose and inorganic phosphate [uncultured organism],4UDK_D Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.76 Angstrom from unknown human gut bacteria (Uhgb_MP) in complex with N-acetyl-D-glucosamine, beta-D-mannopyranose and inorganic phosphate [uncultured organism],4UDK_F Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.76 Angstrom from unknown human gut bacteria (Uhgb_MP) in complex with N-acetyl-D-glucosamine, beta-D-mannopyranose and inorganic phosphate [uncultured organism]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
E6UIS7 1.95e-194 15 389 12 386
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 2.78e-164 4 390 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 4.51e-22 51 361 28 329
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
Q8A8Y4 1.42e-17 51 364 20 319
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
B0K2C3 8.00e-16 71 357 25 300
Beta-1,2-mannobiose phosphorylase OS=Thermoanaerobacter sp. (strain X514) OX=399726 GN=Teth514_1789 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
1.000058 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004560_01693.