logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003402_00758

You are here: Home > Sequence: MGYG000003402_00758

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 Paenibacillus lactis
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus lactis
CAZyme ID MGYG000003402_00758
CAZy Family GH74
CAZyme Description Xyloglucanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
787 85531.76 6.3458
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003402 5924245 MAG United States North America
Gene Location Start: 733;  End: 3096  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.151 3.2.1.150 3.2.1.- 3.2.1.4

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH74 41 180 2.1e-27 0.5836909871244635
GH74 546 669 2.5e-21 0.5064377682403434

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 1.40e-08 141 326 51 250
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
cd15482 Sialidase_non-viral 2.66e-06 86 320 48 300
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
pfam15902 Sortilin-Vps10 8.58e-06 535 689 6 167
Sortilin, neurotensin receptor 3,. Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
pfam15902 Sortilin-Vps10 2.93e-05 199 316 1 112
Sortilin, neurotensin receptor 3,. Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
cd15482 Sialidase_non-viral 3.03e-05 68 249 157 332
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ANY71781.1 0.0 1 739 52 790
AFH63859.2 0.0 1 733 54 785
AEI43924.1 0.0 1 733 54 785
AFC31516.1 0.0 1 733 54 785
AOZ92593.1 0.0 1 729 56 784

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6MGL_A 3.31e-296 3 723 16 745
Crystalstructure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, D60A mutant in complex with XXLG and XGXXLG xyloglucan [Paenibacillus odorifer]
6P2N_A 9.76e-296 3 723 16 746
Crystalstructure of Paenibacillus graminis GH74 (PgGH74) [Paenibacillus graminis]
6MGJ_A 4.70e-291 3 723 16 745
Crystalstructure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_B Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_C Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_D Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_E Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_F Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_G Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_H Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGK_A Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, in complex with XLX xyloglucan [Paenibacillus odorifer],6MGK_B Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, in complex with XLX xyloglucan [Paenibacillus odorifer],6MGK_C Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, in complex with XLX xyloglucan [Paenibacillus odorifer],6MGK_D Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, in complex with XLX xyloglucan [Paenibacillus odorifer]
2CN3_A 3.79e-290 3 727 21 734
ChainA, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN3_B Chain B, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus]
2CN2_A 4.36e-284 3 727 21 734
ChainA, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN2_B Chain B, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN2_C Chain C, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN2_D Chain D, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q3MUH7 2.15e-308 3 734 48 776
Xyloglucanase OS=Paenibacillus sp. OX=58172 GN=xeg74 PE=1 SV=1
A3DFA0 1.24e-289 3 727 48 761
Xyloglucanase Xgh74A OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=xghA PE=3 SV=1
Q70DK5 4.99e-289 3 727 48 761
Xyloglucanase Xgh74A OS=Acetivibrio thermocellus OX=1515 GN=xghA PE=1 SV=1
Q7Z9M8 4.84e-164 3 719 31 740
Xyloglucanase OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=cel74a PE=1 SV=1
A1DAU0 7.43e-149 1 731 34 808
Probable oligoxyloglucan-reducing end-specific xyloglucanase OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=xgcA PE=3 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
0.999876 0.000156 0.000004 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003402_00758.