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CAZyme Information: MGYG000000152_01857

You are here: Home > Sequence: MGYG000000152_01857

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 Lacrimispora sp902363835
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lacrimispora; Lacrimispora sp902363835
CAZyme ID MGYG000000152_01857
CAZy Family GH95
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
989 MGYG000000152_7|CGC2 113109.52 5.8064
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000152 6260407 Isolate United Kingdom Europe
Gene Location Start: 82796;  End: 85765  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000152_01857.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH95 302 740 9.1e-72 0.5692520775623269

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam14498 Glyco_hyd_65N_2 4.19e-05 12 41 9 38
Glycosyl hydrolase family 65, N-terminal domain. This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain.
COG1554 ATH1 0.003 418 537 443 550
Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
pfam03632 Glyco_hydro_65m 0.003 418 459 125 167
Glycosyl hydrolase family 65 central catalytic domain. This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom. The catalytic domain also forms the majority of the dimerization interface.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QOV19156.1 1.25e-314 2 984 3 995
QDM42075.1 1.72e-46 418 708 1 295
QDM42074.1 2.43e-31 290 394 3 107
QRM69892.1 2.96e-29 4 742 32 727
QKH84925.1 2.96e-29 4 742 32 727

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7KMQ_A 2.01e-10 3 602 42 663
ChainA, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306],7KMQ_B Chain B, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8L7W8 9.01e-15 305 619 390 723
Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 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
1.000078 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000152_01857.