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CAZyme Information: MGYG000001851_00329

You are here: Home > Sequence: MGYG000001851_00329

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
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-552; UMGS1880;
CAZyme ID MGYG000001851_00329
CAZy Family GH3
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1407 150953.27 4.1355
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001851 1612023 MAG Denmark Europe
Gene Location Start: 6034;  End: 10257  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001851_00329.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH3 822 1055 2.2e-39 0.9675925925925926

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK15098 PRK15098 2.21e-13 445 546 632 730
beta-glucosidase BglX.
pfam01915 Glyco_hydro_3_C 6.98e-13 76 342 2 184
Glycosyl hydrolase family 3 C-terminal domain. This domain is involved in catalysis and may be involved in binding beta-glucan. This domain is found associated with pfam00933.
pfam14310 Fn3-like 1.81e-12 498 577 1 71
Fibronectin type III-like domain. This domain has a fibronectin type III-like structure. It is often found in association with pfam00933 and pfam01915. Its function is unknown.
pfam01391 Collagen 6.70e-11 1306 1371 1 55
Collagen triple helix repeat (20 copies). Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
pfam00933 Glyco_hydro_3 1.37e-07 859 1057 86 283
Glycosyl hydrolase family 3 N terminal domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
VEU80232.1 3.43e-166 48 1119 65 917
VEU80230.1 9.95e-158 49 1213 29 996
QFJ55185.1 6.36e-154 46 1058 58 918
SQH20118.1 6.82e-138 43 1120 54 922
ASE08187.2 6.82e-138 43 1120 54 922

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5WUG_A 9.12e-54 60 1055 33 776
Expression,characterization and crystal structure of a novel beta-glucosidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii],5WVP_A Expression, characterization and crystal structure of a novel beta-glucosidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
2X42_A 2.33e-26 73 577 334 702
Structureof beta-glucosidase 3B from Thermotoga neapolitana in complex with alpha-D-glucose [Thermotoga neapolitana DSM 4359]
2X40_A 2.33e-26 73 577 334 702
Structureof beta-glucosidase 3B from Thermotoga neapolitana in complex with glycerol [Thermotoga neapolitana DSM 4359],2X41_A Structure of beta-glucosidase 3B from Thermotoga neapolitana in complex with glucose [Thermotoga neapolitana DSM 4359]
7MS2_A 1.77e-22 261 573 418 653
ChainA, Thermostable beta-glucosidase B [Acetivibrio thermocellus AD2],7MS2_B Chain B, Thermostable beta-glucosidase B [Acetivibrio thermocellus AD2]
5WAB_A 2.09e-21 796 1047 9 251
CrystalStructure of Bifidobacterium adolescentis GH3 beta-glucosidase [Bifidobacterium adolescentis ATCC 15703],5WAB_B Crystal Structure of Bifidobacterium adolescentis GH3 beta-glucosidase [Bifidobacterium adolescentis ATCC 15703],5WAB_C Crystal Structure of Bifidobacterium adolescentis GH3 beta-glucosidase [Bifidobacterium adolescentis ATCC 15703],5WAB_D Crystal Structure of Bifidobacterium adolescentis GH3 beta-glucosidase [Bifidobacterium adolescentis ATCC 15703]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P16084 1.86e-61 189 1034 130 769
Beta-glucosidase A OS=Butyrivibrio fibrisolvens OX=831 GN=bglA PE=3 SV=1
P15885 1.36e-34 271 1096 151 752
Beta-glucosidase OS=Ruminococcus albus OX=1264 PE=3 SV=1
P27034 5.92e-24 793 1040 3 228
Beta-glucosidase OS=Rhizobium radiobacter OX=358 GN=cbg-1 PE=3 SV=1
P14002 9.71e-22 261 573 418 653
Thermostable beta-glucosidase B OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=bglB PE=1 SV=2
Q2U9M7 1.10e-21 865 1047 67 242
Probable beta-glucosidase H OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=bglH PE=3 SV=2

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
0.074769 0.922173 0.002203 0.000330 0.000241 0.000252

TMHMM  Annotations      download full data without filtering help

start end
13 35
1379 1401