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CAZyme Information: MGYG000003916_00730

You are here: Home > Sequence: MGYG000003916_00730

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 UMGS1474 sp900547105
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1474; UMGS1474 sp900547105
CAZyme ID MGYG000003916_00730
CAZy Family CBM32
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1241 MGYG000003916_4|CGC1 136727.66 4.4614
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003916 2239460 MAG China Asia
Gene Location Start: 42601;  End: 46326  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003916_00730.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH2 341 1115 5.8e-88 0.8231382978723404
CBM32 229 319 1.7e-16 0.7338709677419355

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3250 LacZ 4.59e-44 377 877 30 493
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
pfam18368 Ig_GlcNase 1.40e-33 1050 1159 1 104
Exo-beta-D-glucosaminidase Ig-fold domain. This domain can be found in 2 glycoside hydrolase subfamily of beta-glucosaminidases (EC:3.2.1.165) such as CsxA, from Amycolatopsis orientalis that has exo-beta-D-glucosaminidase (exo-chitosanase) activity. It has an immunoglobulin-like topology.
pfam00703 Glyco_hydro_2 1.53e-14 545 659 1 106
Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
PRK10150 PRK10150 3.24e-13 370 805 28 443
beta-D-glucuronidase; Provisional
cd14256 Dockerin_I 8.92e-12 1171 1225 1 55
Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCI59726.1 0.0 1 1164 1 1319
BCI60689.1 0.0 6 1159 7 1199
BCI59728.1 0.0 15 1166 13 1223
QOY90771.1 1.30e-271 9 1159 11 1162
BAR52607.1 2.27e-267 32 1159 67 1208

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VZO_A 1.25e-76 333 1175 40 907
Crystalstructure of Amycolatopsis orientalis exo-chitosanase CsxA [Amycolatopsis orientalis],2VZO_B Crystal structure of Amycolatopsis orientalis exo-chitosanase CsxA [Amycolatopsis orientalis]
2VZS_A 3.07e-76 333 1175 40 907
ChitosanProduct complex of Amycolatopsis orientalis exo-chitosanase CsxA [Amycolatopsis orientalis],2VZS_B Chitosan Product complex of Amycolatopsis orientalis exo-chitosanase CsxA [Amycolatopsis orientalis],2X05_A Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine- configured castanospermine and an amino-australine analogue [Amycolatopsis orientalis],2X05_B Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine- configured castanospermine and an amino-australine analogue [Amycolatopsis orientalis],2X09_A Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine- configured castanospermine and an amino-australine analogue [Amycolatopsis orientalis],2X09_B Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine- configured castanospermine and an amino-australine analogue [Amycolatopsis orientalis]
2VZT_A 7.53e-76 333 1175 40 907
Complexof Amycolatopsis orientalis exo-chitosanase CsxA E541A with PNP-beta-D-glucosamine [Amycolatopsis orientalis],2VZT_B Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with PNP-beta-D-glucosamine [Amycolatopsis orientalis],2VZV_A Substrate Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with chitosan [Amycolatopsis orientalis],2VZV_B Substrate Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with chitosan [Amycolatopsis orientalis]
2VZU_A 8.19e-75 333 1175 40 907
Complexof Amycolatopsis orientalis exo-chitosanase CsxA D469A with PNP-beta-D-glucosamine [Amycolatopsis orientalis],2VZU_B Complex of Amycolatopsis orientalis exo-chitosanase CsxA D469A with PNP-beta-D-glucosamine [Amycolatopsis orientalis]
2VJX_A 2.00e-40 369 1132 18 810
Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VJX_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VQT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VR4_A Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482],2VR4_B Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [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
Q82NR8 9.70e-91 334 1158 41 895
Exo-beta-D-glucosaminidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=csxA PE=1 SV=1
Q5H7P5 7.23e-89 343 1158 2 944
Mannosylglycoprotein endo-beta-mannosidase OS=Lilium longiflorum OX=4690 GN=EBM PE=1 SV=4
Q75W54 3.81e-83 352 1158 13 935
Mannosylglycoprotein endo-beta-mannosidase OS=Arabidopsis thaliana OX=3702 GN=EBM PE=1 SV=3
Q56F26 3.06e-75 333 1175 40 907
Exo-beta-D-glucosaminidase OS=Amycolatopsis orientalis OX=31958 GN=csxA PE=1 SV=2
Q4R1C4 1.26e-57 351 1164 37 890
Exo-beta-D-glucosaminidase OS=Hypocrea jecorina OX=51453 GN=gls93 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.002098 0.878842 0.117556 0.000917 0.000325 0.000241

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003916_00730.