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CAZyme Information: MGYG000001798_00762

You are here: Home > Sequence: MGYG000001798_00762

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 Ruminococcus_D sp900752625
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_D; Ruminococcus_D sp900752625
CAZyme ID MGYG000001798_00762
CAZy Family GH74
CAZyme Description Xyloglucanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
758 MGYG000001798_8|CGC1 83177.45 3.981
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001798 2367577 MAG Denmark Europe
Gene Location Start: 46235;  End: 48511  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 107 213 1.7e-21 0.463519313304721
GH74 594 739 1.9e-17 0.4334763948497854

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam15902 Sortilin-Vps10 2.32e-07 144 268 5 112
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.
pfam15902 Sortilin-Vps10 7.43e-06 98 209 13 115
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 2.16e-05 523 626 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.
smart00602 VPS10 3.08e-04 140 203 55 112
VPS10 domain.
cd15482 Sialidase_non-viral 0.001 511 626 162 296
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
CCO05647.1 0.0 1 758 1 762
ADU20593.1 0.0 2 757 3 768
CBL16561.1 8.28e-188 53 758 34 727
ANY71781.1 7.05e-183 49 758 41 777
AGF55626.1 2.12e-181 49 755 38 782

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6MGL_A 1.74e-166 53 752 6 742
Crystalstructure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, D60A mutant in complex with XXLG and XGXXLG xyloglucan [Paenibacillus odorifer]
6MGJ_A 4.78e-163 53 752 6 742
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 5.00e-163 53 754 11 729
ChainA, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN3_B Chain B, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus]
2CN2_A 7.84e-162 53 754 11 729
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]
6P2N_A 1.49e-158 53 752 6 743
Crystalstructure of Paenibacillus graminis GH74 (PgGH74) [Paenibacillus graminis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A3DFA0 9.62e-163 53 754 38 756
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
Q3MUH7 1.67e-162 53 752 38 762
Xyloglucanase OS=Paenibacillus sp. OX=58172 GN=xeg74 PE=1 SV=1
Q70DK5 3.80e-162 53 754 38 756
Xyloglucanase Xgh74A OS=Acetivibrio thermocellus OX=1515 GN=xghA PE=1 SV=1
A1DAU0 3.79e-126 50 756 24 798
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
Q5BD38 2.09e-123 53 758 35 810
Oligoxyloglucan-reducing end-specific xyloglucanase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=xgcA 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 1.000045 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001798_00762.