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CAZyme Information: MGYG000003662_01958

You are here: Home > Sequence: MGYG000003662_01958

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 Prevotella sp900771975
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900771975
CAZyme ID MGYG000003662_01958
CAZy Family GH5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
500 MGYG000003662_72|CGC2 56012.44 4.613
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003662 2760601 MAG Peru South America
Gene Location Start: 74714;  End: 76216  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.73 3.2.1.78 3.2.1.4 3.2.1.8 3.2.1.151

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 186 476 2.7e-87 0.9818840579710145

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00150 Cellulase 2.03e-42 186 475 16 266
Cellulase (glycosyl hydrolase family 5).
COG2730 BglC 1.82e-15 185 475 66 357
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948 BACON 1.53e-12 45 133 7 82
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
pfam13004 BACON 8.94e-05 67 133 1 60
Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.
pfam19190 BACON_2 6.07e-04 45 135 7 90
Viral BACON domain. This family represents a distinct class of BACON domains found in crAss-like phages, the most common viral family in the human gut, in which they are found in tail fiber genes. This suggests they may play a role in phage-host interactions.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QPB75690.1 1.45e-179 10 495 1 497
QRX63738.1 3.87e-91 11 500 13 480
AAA22909.1 1.69e-82 131 495 12 357
BCS86234.1 1.77e-81 131 495 414 770
AEX97596.1 6.18e-80 151 495 39 375

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5D9N_A 4.55e-84 131 495 2 347
Crystalstructure of PbGH5A, a glycoside hydrolase family 5 member from Prevotella bryantii B14, in complex with the xyloglucan heptasaccharide XXXG [Prevotella bryantii],5D9N_B Crystal structure of PbGH5A, a glycoside hydrolase family 5 member from Prevotella bryantii B14, in complex with the xyloglucan heptasaccharide XXXG [Prevotella bryantii],5D9P_A Crystal structure of PbGH5A, a glycoside hydrolase family 5 enzyme from Prevotella bryantii B14, in complex with an inhibitory N-bromoacetylglycosylamine derivative of XXXG [Prevotella bryantii],5D9P_B Crystal structure of PbGH5A, a glycoside hydrolase family 5 enzyme from Prevotella bryantii B14, in complex with an inhibitory N-bromoacetylglycosylamine derivative of XXXG [Prevotella bryantii]
5D9M_A 3.57e-83 131 495 2 347
Crystalstructure of PbGH5A, a glycoside hydrolase family 5 enzyme from Prevotella bryantii B14, E280A mutant in complex with the xyloglucan tetradecasaccharide XXXGXXXG [Prevotella bryantii],5D9M_B Crystal structure of PbGH5A, a glycoside hydrolase family 5 enzyme from Prevotella bryantii B14, E280A mutant in complex with the xyloglucan tetradecasaccharide XXXGXXXG [Prevotella bryantii],5D9O_A Crystal structure of PbGH5A, a glycoside hydrolase family 5 enzyme from Prevotella bryantii B14, E280A mutant in complex with cellotetraose [Prevotella bryantii],5D9O_B Crystal structure of PbGH5A, a glycoside hydrolase family 5 enzyme from Prevotella bryantii B14, E280A mutant in complex with cellotetraose [Prevotella bryantii]
6D2W_A 7.05e-80 126 495 411 770
Crystalstructure of Prevotella bryantii endo-beta-mannanase/endo-beta-glucanase PbGH26A-GH5A [Prevotella bryantii B14],6D2W_B Crystal structure of Prevotella bryantii endo-beta-mannanase/endo-beta-glucanase PbGH26A-GH5A [Prevotella bryantii B14]
3VDH_A 1.90e-79 145 494 11 346
Crystalstructure of PbGH5A, a glycoside hydrolase family 5 enzyme from Prevotella bryantii B14 [Prevotella bryantii],3VDH_B Crystal structure of PbGH5A, a glycoside hydrolase family 5 enzyme from Prevotella bryantii B14 [Prevotella bryantii]
6WQP_A 8.98e-60 150 495 19 352
GH5-4broad specificity endoglucanase from Ruminococcus champanellensis [Ruminococcus champanellensis],6WQP_B GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis [Ruminococcus champanellensis],6WQV_A GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_B GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_C GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_D GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P54937 2.56e-51 111 495 4 374
Endoglucanase A OS=Clostridium longisporum OX=1523 GN=celA PE=1 SV=1
P20847 8.34e-50 146 495 38 391
Endoglucanase 1 OS=Butyrivibrio fibrisolvens OX=831 GN=end1 PE=3 SV=1
P23660 9.86e-49 146 500 26 364
Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA PE=1 SV=1
P23661 2.03e-48 141 494 63 395
Endoglucanase B OS=Ruminococcus albus OX=1264 GN=celB PE=3 SV=1
P17901 2.17e-48 141 495 41 396
Endoglucanase A OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=celCCA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000074 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003662_01958.