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CAZyme Information: MGYG000000456_00584

You are here: Home > Sequence: MGYG000000456_00584

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; Oscillospirales; Acutalibacteraceae; ;
CAZyme ID MGYG000000456_00584
CAZy Family GH92
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
734 MGYG000000456_70|CGC1 82943.54 4.7431
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000456 2140419 MAG Sweden Europe
Gene Location Start: 364;  End: 2568  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.113

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH92 217 718 2.2e-164 0.9877800407331976

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3537 COG3537 0.0 4 732 39 758
Putative alpha-1,2-mannosidase [Carbohydrate transport and metabolism].
pfam07971 Glyco_hydro_92 0.0 241 715 1 464
Glycosyl hydrolase family 92. Members of this family are alpha-1,2-mannosidases, enzymes which remove alpha-1,2-linked mannose residues from Man(9)(GlcNAc)(2) by hydrolysis. They are critical for the maturation of N-linked oligosaccharides and ER-associated degradation.
TIGR01180 aman2_put 5.80e-102 4 718 35 748
alpha-1,2-mannosidase, putative. The identification of members of this family as putative alpha-1,2-mannosidases is based on an unpublished characterization of the aman2 gene in Bacillus sp. M-90 by Maruyama,Y., Nakajima,M. and Nakajima,T. (Genbank accession BAA76709, pid g4587313). Most members of this family appear to have signal sequences. Members from the dental pathogen Porphyromonas gingivalis have been described as immunoreactive with periodontitis patient serum. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
NF035929 lectin_1 2.60e-42 5 718 9 684
lectin. Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.
pfam17678 Glyco_hydro_92N 1.36e-18 6 235 1 231
Glycosyl hydrolase family 92 N-terminal domain. This domain is found at the N-terminus of family 92 glycosyl hydrolase proteins.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBI31946.1 5.08e-234 1 734 1 734
SMF64542.1 2.70e-227 7 734 5 729
ACX68331.1 2.82e-224 4 734 2 729
QOT09581.1 4.00e-224 4 734 2 729
AYB47488.1 1.13e-223 4 734 2 729

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7FE1_A 3.55e-191 4 733 3 710
ChainA, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE1_B Chain B, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE1_C Chain C, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE1_D Chain D, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100]
6DWO_A 7.10e-191 4 733 3 710
Crystalstructure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],6DWO_B Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],6DWO_C Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],6DWO_D Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583]
7FE2_A 1.00e-190 4 733 3 710
ChainA, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE2_B Chain B, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE2_C Chain C, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE2_D Chain D, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100]
2WZS_A 2.84e-177 3 734 3 735
Structureof the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with Mannoimidazole [Bacteroides thetaiotaomicron VPI-5482],2WZS_B Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with Mannoimidazole [Bacteroides thetaiotaomicron VPI-5482],2WZS_C Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with Mannoimidazole [Bacteroides thetaiotaomicron VPI-5482],2WZS_D Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with Mannoimidazole [Bacteroides thetaiotaomicron VPI-5482],2WZS_E Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with Mannoimidazole [Bacteroides thetaiotaomicron VPI-5482],2WZS_F Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with Mannoimidazole [Bacteroides thetaiotaomicron VPI-5482],2WZS_G Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with Mannoimidazole [Bacteroides thetaiotaomicron VPI-5482],2WZS_H Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with Mannoimidazole [Bacteroides thetaiotaomicron VPI-5482]
2WVZ_A 3.42e-177 3 734 3 735
Structureof the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WVZ_B Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WVZ_C Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WVZ_D Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW0_A Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW0_B Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW0_C Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW0_D Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW0_E Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW0_F Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW0_G Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW0_H Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW1_A Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with Thiomannobioside [Bacteroides thetaiotaomicron VPI-5482],2WW1_B Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with Thiomannobioside [Bacteroides thetaiotaomicron VPI-5482],2WW1_C Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with Thiomannobioside [Bacteroides thetaiotaomicron VPI-5482],2WW1_D Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with Thiomannobioside [Bacteroides thetaiotaomicron VPI-5482],2WW3_A Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with thiomannobioside [Bacteroides thetaiotaomicron VPI-5482],2WW3_B Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with thiomannobioside [Bacteroides thetaiotaomicron VPI-5482],2WW3_C Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with thiomannobioside [Bacteroides thetaiotaomicron VPI-5482],2WW3_D Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with thiomannobioside [Bacteroides thetaiotaomicron VPI-5482],2WW3_E Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with thiomannobioside [Bacteroides thetaiotaomicron VPI-5482],2WW3_F Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 in complex with thiomannobioside [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O86365 3.41e-53 4 719 42 754
Uncharacterized glycosidase Rv0584 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv0584 PE=3 SV=1
D4ATR3 1.26e-38 213 732 261 758
Uncharacterized secreted glycosidase ARB_07629 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07629 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
1.000031 0.000006 0.000001 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000456_00584.