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CAZyme Information: MGYG000001275_00172

You are here: Home > Sequence: MGYG000001275_00172

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 CAG-485 sp900321585
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900321585
CAZyme ID MGYG000001275_00172
CAZy Family GH5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
576 MGYG000001275_2|CGC1 63301.8 4.6055
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001275 2994513 MAG Italy Europe
Gene Location Start: 34713;  End: 36443  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001275_00172.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 248 544 5.9e-91 0.9855072463768116

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00150 Cellulase 1.37e-47 242 543 10 267
Cellulase (glycosyl hydrolase family 5).
COG2730 BglC 5.02e-18 236 501 55 322
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948 BACON 7.40e-12 34 119 1 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.
cd14948 BACON 4.54e-11 135 212 10 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 3.80e-07 62 119 4 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
QCD42340.1 5.27e-138 3 576 13 593
SCD22090.1 2.02e-124 11 576 11 566
SCM57160.1 8.01e-124 11 576 11 566
QQA29804.1 3.39e-110 17 576 24 593
QUT65987.1 6.73e-110 17 576 24 593

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5OYC_A 3.21e-98 217 569 38 393
GH5endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYC_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYD_A GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYD_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYE_A GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYE_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107]
6HA9_A 2.52e-97 217 569 38 393
Structureof an endo-Xyloglucanase from Cellvibrio japonicus complexed with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HA9_B Structure of an endo-Xyloglucanase from Cellvibrio japonicus complexed with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HAA_A Structure of a covalent complex of endo-Xyloglucanase from Cellvibrio japonicus after reacting with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HAA_B Structure of a covalent complex of endo-Xyloglucanase from Cellvibrio japonicus after reacting with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107]
4W8A_A 6.50e-70 237 576 15 378
Crystalstructure of XEG5B, a GH5 xyloglucan-specific beta-1,4-glucanase from ruminal metagenomic library, in the native form [uncultured bacterium],4W8B_A Crystal structure of XEG5B, a GH5 xyloglucan-specific beta-1,4-glucanase from ruminal metagenomic library, in complex with XXLG [uncultured bacterium]
3ZMR_A 1.04e-66 127 568 10 465
Bacteroidesovatus GH5 xyloglucanase in complex with a XXXG heptasaccharide [Bacteroides ovatus],3ZMR_B Bacteroides ovatus GH5 xyloglucanase in complex with a XXXG heptasaccharide [Bacteroides ovatus]
2JEP_A 2.09e-48 237 568 47 393
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A7LXT7 1.09e-65 127 568 45 500
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
O08342 2.29e-44 237 568 52 398
Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
P10477 9.15e-39 219 569 51 385
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
P28623 3.28e-38 213 563 31 358
Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2
P23660 1.43e-37 222 549 24 340
Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA 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 0.000009 1.000044 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001275_00172.