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CAZyme Information: MGYG000001728_00513

You are here: Home > Sequence: MGYG000001728_00513

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 sp002305315
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; UBA1390; UBA1390; UBA1390 sp002305315
CAZyme ID MGYG000001728_00513
CAZy Family GH95
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
787 MGYG000001728_55|CGC1 89229.56 4.9748
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001728 2194259 MAG Sweden Europe
Gene Location Start: 3057;  End: 5420  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001728_00513.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH95 7 754 4.1e-160 0.9709141274238227

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam14498 Glyco_hyd_65N_2 2.17e-30 8 242 4 225
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 1.76e-09 108 554 96 548
Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
pfam03632 Glyco_hydro_65m 7.48e-05 385 593 58 272
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 1.46e-247 2 785 8 792
QGH32985.1 2.35e-246 5 761 11 763
QKS45791.1 1.24e-241 5 756 11 758
ANY73534.1 4.75e-240 3 757 5 785
AYB47098.1 8.27e-238 3 772 5 800

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7KMQ_A 3.61e-50 13 753 44 757
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 6.71e-48 18 739 14 737
ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
4UFC_A 3.13e-47 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]
2EAB_A 2.97e-28 18 773 47 869
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]
2EAD_A 1.20e-27 18 773 47 869
ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [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 2.83e-61 18 731 63 789
Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
A2R797 4.52e-42 21 733 38 757
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
1.000073 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001728_00513.