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CAZyme Information: MGYG000000997_00479

You are here: Home > Sequence: MGYG000000997_00479

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 Roseburia sp900548205
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia sp900548205
CAZyme ID MGYG000000997_00479
CAZy Family GH95
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
745 MGYG000000997_7|CGC1 85275.13 6.115
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000997 2319952 MAG China Asia
Gene Location Start: 29720;  End: 31957  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000997_00479.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH95 4 713 3.5e-108 0.9764542936288089

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam14498 Glyco_hyd_65N_2 5.39e-08 9 161 5 164
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 2.12e-04 414 514 443 548
Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
pfam03632 Glyco_hydro_65m 0.007 417 514 128 229
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
QUH27705.1 4.94e-251 5 725 16 730
AZN43093.1 9.63e-244 2 712 10 707
QJD87118.1 3.90e-234 2 703 12 706
ARU44480.1 6.76e-173 5 705 32 723
AFD08908.1 1.01e-167 2 705 27 720

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7KMQ_A 7.71e-32 4 705 42 751
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]
2RDY_A 1.29e-29 4 707 4 748
ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
4UFC_A 5.44e-25 4 696 23 726
Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8L7W8 1.63e-32 4 701 53 802
Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
A2R797 1.96e-16 295 697 351 762
Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA 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
1.000061 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000997_00479.