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CAZyme Information: MGYG000001095_02386

You are here: Home > Sequence: MGYG000001095_02386

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 Chryseobacterium gambrini
Lineage Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; Weeksellaceae; Chryseobacterium; Chryseobacterium gambrini
CAZyme ID MGYG000001095_02386
CAZy Family GH2
CAZyme Description Exo-beta-D-glucosaminidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
826 MGYG000001095_392|CGC1 96106.29 6.7054
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001095 4128611 MAG Sweden Europe
Gene Location Start: 1781;  End: 4261  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.25

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH2 22 768 2.4e-110 0.7473404255319149

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3250 LacZ 1.27e-112 27 665 16 643
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10150 PRK10150 1.24e-13 30 436 19 419
beta-D-glucuronidase; Provisional
PRK10340 ebgA 1.60e-12 81 434 113 449
cryptic beta-D-galactosidase subunit alpha; Reviewed
pfam00703 Glyco_hydro_2 8.74e-12 204 303 1 106
Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
pfam17753 Ig_mannosidase 1.77e-10 760 823 1 78
Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AZA97484.1 0.0 1 826 1 826
QWA38544.1 0.0 1 826 1 827
ALR29845.1 0.0 1 826 1 827
VFB03094.1 0.0 1 826 1 826
QQV03575.1 0.0 1 826 1 826

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VJX_A 6.84e-235 21 812 6 819
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]
2JE8_A 7.30e-235 21 812 8 821
Structureof a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JE8_B Structure of a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
7OP6_A 7.54e-235 21 812 8 821
ChainA, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP6_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_A Chain A, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482]
2WBK_A 2.00e-234 21 812 6 819
Structureof the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482],2WBK_B Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482]
2VQU_A 8.78e-233 21 812 6 819
Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQU_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q4FZV0 5.57e-121 30 822 29 872
Beta-mannosidase OS=Rattus norvegicus OX=10116 GN=Manba PE=2 SV=1
Q5B7W2 4.62e-120 23 650 6 651
Beta-mannosidase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=mndB PE=1 SV=2
Q0CCA0 6.47e-120 18 650 2 649
Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
Q8K2I4 1.60e-118 27 822 26 870
Beta-mannosidase OS=Mus musculus OX=10090 GN=Manba PE=1 SV=1
Q95327 1.60e-118 30 673 29 709
Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA 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
0.001768 0.997361 0.000311 0.000186 0.000177 0.000176

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001095_02386.