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CAZyme Information: MGYG000004899_02664

You are here: Home > Sequence: MGYG000004899_02664

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 sp900555635
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900555635
CAZyme ID MGYG000004899_02664
CAZy Family GH5
CAZyme Description Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
476 MGYG000004899_14|CGC2 53379.54 4.8969
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004899 5396709 MAG China Asia
Gene Location Start: 106163;  End: 107593  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004899_02664.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 161 444 1.2e-80 0.9891304347826086

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00150 Cellulase 1.40e-40 146 415 1 242
Cellulase (glycosyl hydrolase family 5).
COG2730 BglC 1.08e-21 114 409 29 321
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948 BACON 1.30e-17 24 107 1 83
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 4.19e-05 49 107 1 61
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 6.84e-05 24 109 1 91
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
QBJ18101.1 1.11e-258 2 475 7 477
QMI79558.1 1.57e-258 2 475 7 477
QUT65254.1 5.03e-258 2 475 10 480
QUT33510.1 5.03e-258 2 475 10 480
QUT61941.1 9.07e-258 2 475 7 477

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6XRK_A 5.41e-62 128 470 23 372
GH5-4broad specificity endoglucanase from an uncultured bovine rumen ciliate [uncultured bovine rumen ciliate],6XRK_B GH5-4 broad specificity endoglucanase from an uncultured bovine rumen ciliate [uncultured bovine rumen ciliate]
4IM4_A 4.25e-55 132 466 10 332
ChainA, Endoglucanase E [Acetivibrio thermocellus],4IM4_B Chain B, Endoglucanase E [Acetivibrio thermocellus],4IM4_C Chain C, Endoglucanase E [Acetivibrio thermocellus],4IM4_D Chain D, Endoglucanase E [Acetivibrio thermocellus],4IM4_E Chain E, Endoglucanase E [Acetivibrio thermocellus],4IM4_F Chain F, Endoglucanase E [Acetivibrio thermocellus]
6WQP_A 5.65e-52 126 467 13 354
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]
3NDY_A 6.28e-52 123 459 7 331
Thestructure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDZ_A The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans]
4X0V_A 3.08e-51 126 467 37 393
Structureof a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_B Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_C Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_D Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_E Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_F Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_G Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_H Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P10477 5.20e-51 132 466 60 382
Cellulase/esterase CelE OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celE PE=1 SV=2
A7LXT7 1.58e-50 14 443 31 473
Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02653 PE=1 SV=1
P28623 1.04e-49 123 459 38 362
Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2
P23660 3.07e-49 123 442 22 327
Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA PE=1 SV=1
P17901 2.53e-47 133 467 51 398
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 0.000006 1.000070 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004899_02664.