dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Bacteroides sp900556215

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900556215

CAZyme ID

MGYG000000211_00518

CAZy Family

GH130

CAZyme Description

1,4-beta-mannosyl-N-acetylglucosamine phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
361	MGYG000000211_1\|CGC17	41690.65	6.933

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000211	6486320	Isolate	China	Asia

Gene Location

Start: 787289; End: 788374 Strand: -

Enzyme Prediction help

EC	2.4.1.-

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH130	27	357	3.3e-99	0.9966216216216216

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18614	GH130	6.19e-121	44	349	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	6.36e-90	44	347	1	269	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.
cd18612	GH130_Lin0857-like	2.95e-80	44	346	1	259	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.
cd08993	GH130	1.32e-78	48	353	5	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.
COG2152	COG2152	2.13e-77	24	361	2	314	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
ARV07990.1	1.29e-200	25	361	1	337
QWG01387.1	5.59e-178	25	361	1	337
QUI21650.1	4.48e-153	25	356	1	330
BCA49031.1	3.61e-149	25	357	1	336
AIM60094.1	4.03e-148	19	358	6	347

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7FIP_A	6.39e-48	27	339	15	298	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	2.69e-43	77	361	108	355	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	8.58e-42	29	360	38	337	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	2.33e-26	29	361	29	334	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	1.80e-24	137	360	119	345	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	7.96e-56	27	339	4	281	1,2-beta-oligomannan phosphorylase OS=Thermoanaerobacter sp. (strain X514) OX=399726 GN=Teth514_1788 PE=1 SV=1
B0K2C3	2.63e-47	27	339	4	287	Beta-1,2-mannobiose phosphorylase OS=Thermoanaerobacter sp. (strain X514) OX=399726 GN=Teth514_1789 PE=1 SV=1
Q92DF6	1.23e-42	77	361	108	355	Beta-1,2-mannobiose phosphorylase OS=Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262) OX=272626 GN=lin0857 PE=1 SV=1
Q8A8Y4	1.56e-28	29	360	21	320	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
E6UBR9	1.28e-25	29	361	29	334	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

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
0.588018	0.409644	0.001167	0.000454	0.000252	0.000464

TMHMM Annotations help

There is no transmembrane helices in MGYG000000211_00518.

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