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CAZyme Information: MGYG000003312_00641

You are here: Home > Sequence: MGYG000003312_00641

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 Bacteroides sp900547205
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900547205
CAZyme ID MGYG000003312_00641
CAZy Family GH130
CAZyme Description 4-O-beta-D-mannosyl-D-glucose phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
343 MGYG000003312_18|CGC1 39215.93 5.9276
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003312 4657579 MAG Estonia Europe
Gene Location Start: 60781;  End: 61812  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003312_00641.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH130 9 337 5.8e-91 0.9628378378378378

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd18614 GH130 2.10e-113 18 331 1 276
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.
cd18607 GH130 5.68e-77 18 325 1 265
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.
cd18611 GH130 3.28e-65 18 329 1 289
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.
cd18612 GH130_Lin0857-like 9.44e-64 18 327 1 258
Glycoside hydrolase family 130 such as Listeria innocua beta-1,2-mannobiose phosphorylase. This subfamily contains the glycosyl hydrolase family 130 (GH130), as classified by the carbohydrate-active enzymes database (CAZY), enzymes that are phosphorylases and hydrolases for beta-mannosides, and includes Listeria innocua beta-1,2-mannobiose phosphorylase (Lin0857). hey 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. Structure of Lin0857 shows beta-1,2-mannotriose bound in a U-shape, interacting with a phosphate analog at both ends. Lin0857 has a unique dimer structure connected by a loop, with a significant open-close loop displacement observed for substrate entry. A long loop, which is exclusively present in Lin0857, covers the active site to limit the pocket size.
cd18615 GH130 3.15e-60 23 325 8 273
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SCD21651.1 9.36e-172 1 338 1 338
BCS86340.1 1.92e-157 1 343 1 344
AEE53504.1 1.80e-151 1 338 1 339
QNA43326.1 4.18e-151 1 339 1 339
AXE18829.1 6.35e-151 1 339 1 339

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7FIP_A 2.69e-38 17 330 31 307
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]
5B0P_A 8.34e-34 68 338 126 350
Beta-1,2-Mannobiosephosphorylase from Listeria innocua - glycerol complex [Listeria innocua Clip11262],5B0P_B Beta-1,2-Mannobiose phosphorylase from Listeria innocua - glycerol complex [Listeria innocua Clip11262],5B0Q_A beta-1,2-Mannobiose phosphorylase from Listeria innocua - mannose complex [Listeria innocua Clip11262],5B0Q_B beta-1,2-Mannobiose phosphorylase from Listeria innocua - mannose complex [Listeria innocua Clip11262],5B0R_A Beta-1,2-Mannobiose phosphorylase from Listeria innocua - beta-1,2-mannobiose complex [Listeria innocua Clip11262],5B0R_B Beta-1,2-Mannobiose phosphorylase from Listeria innocua - beta-1,2-mannobiose complex [Listeria innocua Clip11262],5B0S_A Beta-1,2-Mannobiose phosphorylase from Listeria innocua - beta-1,2-mannotriose complex [Listeria innocua Clip11262],5B0S_B Beta-1,2-Mannobiose phosphorylase from Listeria innocua - beta-1,2-mannotriose complex [Listeria innocua Clip11262]
1VKD_A 1.02e-31 83 336 118 331
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 7.61e-24 83 343 115 330
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 3.22e-23 168 336 169 339
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
B0K2C2 7.83e-42 1 334 1 294
1,2-beta-oligomannan phosphorylase OS=Thermoanaerobacter sp. (strain X514) OX=399726 GN=Teth514_1788 PE=1 SV=1
B0K2C3 1.14e-37 17 330 20 296
Beta-1,2-mannobiose phosphorylase OS=Thermoanaerobacter sp. (strain X514) OX=399726 GN=Teth514_1789 PE=1 SV=1
Q92DF6 3.94e-33 68 338 126 350
Beta-1,2-mannobiose phosphorylase OS=Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262) OX=272626 GN=lin0857 PE=1 SV=1
E6UBR9 4.17e-23 83 343 115 330
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 2.18e-21 69 336 93 314
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
1.000087 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003312_00641.