logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002126_01785

You are here: Home > Sequence: MGYG000002126_01785

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 UBA1390 sp900764045
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; UBA1390; UBA1390; UBA1390 sp900764045
CAZyme ID MGYG000002126_01785
CAZy Family GH95
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
787 MGYG000002126_42|CGC1 90058.35 5.5228
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002126 2317686 MAG Mongolia Asia
Gene Location Start: 7378;  End: 9741  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002126_01785.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH95 8 736 1.3e-155 0.945983379501385

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam14498 Glyco_hyd_65N_2 2.28e-24 5 243 1 225
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 2.10e-06 384 554 375 548
Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
pfam03632 Glyco_hydro_65m 3.86e-06 383 578 56 262
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
QNF27939.1 3.19e-241 2 756 8 757
QKS45791.1 2.84e-240 5 756 11 758
QGH32985.1 2.90e-231 2 756 8 758
AYB47098.1 2.94e-227 2 756 4 785
QZN78893.1 1.83e-225 2 762 5 794

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7KMQ_A 1.23e-45 1 733 32 738
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]
4UFC_A 5.29e-41 18 732 33 721
Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus]
2RDY_A 9.07e-41 18 736 14 736
ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
2EAD_A 1.46e-26 18 777 47 873
ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum]
2EAB_A 1.93e-26 18 777 47 873
Crystalstructure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAB_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAC_A Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum],2EAC_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8L7W8 3.58e-47 18 743 63 800
Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
A2R797 9.59e-32 14 733 31 757
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
1.000044 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002126_01785.