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CAZyme Information: MGYG000002242_01043

You are here: Home > Sequence: MGYG000002242_01043

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 Treponema_D succinifaciens
Lineage Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D succinifaciens
CAZyme ID MGYG000002242_01043
CAZy Family GH130
CAZyme Description 4-O-beta-D-mannosyl-D-glucose phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
391 43919.75 6.7416
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002242 2466093 MAG Peru South America
Gene Location Start: 7813;  End: 8988  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.281

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH130 49 360 2.8e-88 0.9898648648648649

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08993 GH130 5.27e-96 66 356 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 1.86e-77 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 2.44e-38 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 4.64e-38 68 353 4 276
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.
COG2152 COG2152 3.98e-37 36 361 10 310
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
AEN97397.1 1.96e-232 9 388 8 387
BCJ97190.1 9.74e-232 9 388 7 386
QNM02945.1 3.23e-231 5 391 3 389
VCV21228.1 3.36e-231 5 391 4 390
EEV02552.1 4.04e-231 5 391 9 395

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5AY9_A 1.83e-200 5 388 4 386
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 7.64e-170 3 388 4 389
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 6.47e-29 23 360 27 333
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]
7FIP_A 6.36e-19 55 356 22 311
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]
5AYD_A 2.08e-18 47 360 26 329
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
E6UIS7 1.00e-199 5 388 4 386
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 4.18e-169 3 388 4 389
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
B0K2C3 3.00e-18 55 356 11 300
Beta-1,2-mannobiose phosphorylase OS=Thermoanaerobacter sp. (strain X514) OX=399726 GN=Teth514_1789 PE=1 SV=1
E6UBR9 1.14e-17 47 360 26 329
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 1.54e-16 47 363 18 319
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
1.000073 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002242_01043.