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CAZyme Information: MGYG000002935_00098

You are here: Home > Sequence: MGYG000002935_00098

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 Phocaeicola sp002161765
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp002161765
CAZyme ID MGYG000002935_00098
CAZy Family GH5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
593 MGYG000002935_1|CGC2 64352.73 4.1469
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002935 2727252 MAG Finland Europe
Gene Location Start: 123161;  End: 124942  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.4

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 246 541 1.2e-97 0.9891304347826086

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00150 Cellulase 2.70e-56 237 544 1 272
Cellulase (glycosyl hydrolase family 5).
COG2730 BglC 5.59e-25 217 551 41 370
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948 BACON 2.10e-16 124 207 2 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.
cd14948 BACON 4.24e-16 37 118 3 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 1.70e-08 60 118 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADY35478.1 0.0 5 593 2 592
QUT88430.1 5.12e-258 1 593 1 598
ALJ60576.1 1.80e-222 126 593 41 512
QRX62664.1 1.15e-183 129 593 43 513
AVM57519.1 4.69e-180 129 593 88 563

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6WQY_A 1.65e-221 213 577 17 384
ChainA, Cellulase [Phocaeicola salanitronis DSM 18170]
4YHE_A 7.00e-130 222 593 9 386
NativeBacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a],4YHE_B Native Bacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a]
4YHG_A 5.60e-129 222 593 9 386
NativeBacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a],4YHG_B Native Bacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a]
2JEP_A 7.70e-86 222 575 37 394
Nativefamily 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEP_B Native family 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEQ_A Family 5 xyloglucanase from Paenibacillus pabuli in complex with ligand [Paenibacillus pabuli]
3NDY_A 2.01e-65 214 575 6 341
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O08342 8.81e-82 219 575 39 399
Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
P28623 5.99e-64 214 575 37 372
Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2
P28621 3.87e-63 214 554 36 355
Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1
Q12647 1.84e-55 201 557 6 347
Endoglucanase B OS=Neocallimastix patriciarum OX=4758 GN=CELB PE=2 SV=1
A7LXT7 9.17e-55 18 572 27 499
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

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 0.000002 1.000059 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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