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CAZyme Information: MGYG000001151_00114

You are here: Home > Sequence: MGYG000001151_00114

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_C sp000433635
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp000433635
CAZyme ID MGYG000001151_00114
CAZy Family CBM79
CAZyme Description Xyloglucanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
940 100966.09 4.1146
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001151 2508735 MAG China Asia
Gene Location Start: 7578;  End: 10400  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001151_00114.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14256 Dockerin_I 2.12e-09 867 926 1 57
Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
pfam15902 Sortilin-Vps10 8.87e-07 84 203 7 110
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 7.34e-05 543 662 120 243
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.
pfam00404 Dockerin_1 8.27e-04 868 926 1 56
Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium.
cd15482 Sialidase_non-viral 0.001 560 751 18 237
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
CBL16522.1 2.73e-301 38 789 31 779
ADU23213.1 3.26e-280 35 797 30 792
CBL33465.1 7.73e-117 54 792 71 747
CBK97166.1 5.81e-114 54 792 68 744
QJB32550.1 1.25e-108 54 803 68 755

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6P2L_A 7.02e-90 50 803 9 696
Crystalstructure of Niastella koreensis GH74 (NkGH74) enzyme [Niastella koreensis GR20-10]
6P2M_A 1.85e-69 54 790 17 690
ChainA, Type 3a cellulose-binding domain protein [Caldicellulosiruptor lactoaceticus 6A]
6MGL_A 1.05e-58 55 792 15 745
Crystalstructure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, D60A mutant in complex with XXLG and XGXXLG xyloglucan [Paenibacillus odorifer]
2CN3_A 2.61e-57 56 790 21 728
ChainA, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN3_B Chain B, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus]
6MGJ_A 4.04e-57 55 792 15 745
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q5BD38 4.77e-63 54 792 42 807
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
Q3MUH7 4.15e-62 55 803 47 779
Xyloglucanase OS=Paenibacillus sp. OX=58172 GN=xeg74 PE=1 SV=1
A1DAU0 4.03e-58 54 800 34 805
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
Q70DK5 7.36e-58 56 801 48 767
Xyloglucanase Xgh74A OS=Acetivibrio thermocellus OX=1515 GN=xghA PE=1 SV=1
A3DFA0 1.34e-57 56 801 48 767
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

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000774 0.998090 0.000376 0.000313 0.000218 0.000188

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001151_00114.