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CAZyme Information: MGYG000000423_00125

You are here: Home > Sequence: MGYG000000423_00125

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; TANB77; CAG-508; UBA7001;
CAZyme ID MGYG000000423_00125
CAZy Family GH30
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
446 MGYG000000423_1|CGC1 51509.09 6.8738
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000423 1728758 MAG Sweden Europe
Gene Location Start: 132786;  End: 134126  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000423_00125.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH30 33 438 3.7e-143 0.9903846153846154

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02055 Glyco_hydro_30 9.20e-62 49 376 3 348
Glycosyl hydrolase family 30 TIM-barrel domain.
COG5520 XynC 3.88e-60 25 415 25 400
O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis].
pfam17189 Glyco_hydro_30C 2.72e-12 379 439 1 63
Glycosyl hydrolase family 30 beta sandwich domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QPC45518.1 1.95e-118 18 411 26 414
ABX43757.1 6.86e-118 24 438 20 438
BCN32198.1 4.42e-117 1 438 1 440
ABX41244.1 7.09e-116 1 440 1 441
BCK00978.1 3.32e-115 25 438 19 435

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2WNW_A 1.43e-90 24 411 22 412
Thecrystal structure of SrfJ from salmonella typhimurium [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],2WNW_B The crystal structure of SrfJ from salmonella typhimurium [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
1OGS_A 6.50e-54 35 411 66 463
humanacid-beta-glucosidase [Homo sapiens],1OGS_B human acid-beta-glucosidase [Homo sapiens],1Y7V_A Chain A, Glucosylceramidase [Homo sapiens],1Y7V_B Chain B, Glucosylceramidase [Homo sapiens],2F61_A Crystal structure of partially deglycosylated acid beta-glucosidase [Homo sapiens],2F61_B Crystal structure of partially deglycosylated acid beta-glucosidase [Homo sapiens],2J25_A Partially deglycosylated glucoceramidase [Homo sapiens],2J25_B Partially deglycosylated glucoceramidase [Homo sapiens],2NSX_A Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease [Homo sapiens],2NSX_B Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease [Homo sapiens],2NSX_C Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease [Homo sapiens],2NSX_D Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease [Homo sapiens],2NT0_A Acid-beta-glucosidase low pH, glycerol bound [Homo sapiens],2NT0_B Acid-beta-glucosidase low pH, glycerol bound [Homo sapiens],2NT0_C Acid-beta-glucosidase low pH, glycerol bound [Homo sapiens],2NT0_D Acid-beta-glucosidase low pH, glycerol bound [Homo sapiens],2NT1_A Structure of acid-beta-glucosidase at neutral pH [Homo sapiens],2NT1_B Structure of acid-beta-glucosidase at neutral pH [Homo sapiens],2NT1_C Structure of acid-beta-glucosidase at neutral pH [Homo sapiens],2NT1_D Structure of acid-beta-glucosidase at neutral pH [Homo sapiens],3GXD_A Crystal structure of Apo acid-beta-glucosidase pH 4.5 [Homo sapiens],3GXD_B Crystal structure of Apo acid-beta-glucosidase pH 4.5 [Homo sapiens],3GXD_C Crystal structure of Apo acid-beta-glucosidase pH 4.5 [Homo sapiens],3GXD_D Crystal structure of Apo acid-beta-glucosidase pH 4.5 [Homo sapiens],3GXF_A Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH [Homo sapiens],3GXF_B Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH [Homo sapiens],3GXF_C Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH [Homo sapiens],3GXF_D Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH [Homo sapiens],3GXI_A Crystal structure of acid-beta-glucosidase at pH 5.5 [Homo sapiens],3GXI_B Crystal structure of acid-beta-glucosidase at pH 5.5 [Homo sapiens],3GXI_C Crystal structure of acid-beta-glucosidase at pH 5.5 [Homo sapiens],3GXI_D Crystal structure of acid-beta-glucosidase at pH 5.5 [Homo sapiens],3GXM_A Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition [Homo sapiens],3GXM_B Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition [Homo sapiens],3GXM_C Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition [Homo sapiens],3GXM_D Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition [Homo sapiens],3RIK_A The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIK_B The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIK_C The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIK_D The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIL_A The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIL_B The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIL_C The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIL_D The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],6MOZ_A Structure of acid-beta-glucosidase in complex with an aromatic pyrrolidine iminosugar inhibitor [Homo sapiens],6MOZ_B Structure of acid-beta-glucosidase in complex with an aromatic pyrrolidine iminosugar inhibitor [Homo sapiens],6Q1N_A Glucocerebrosidase in complex with pharmacological chaperone IMX8 [Homo sapiens],6Q1N_B Glucocerebrosidase in complex with pharmacological chaperone IMX8 [Homo sapiens],6Q1P_A Glucocerebrosidase in complex with pharmacological chaperone norIMX8 [Homo sapiens],6Q1P_B Glucocerebrosidase in complex with pharmacological chaperone norIMX8 [Homo sapiens],6Q6K_A Crystal structure of recombinant human beta-glucocerebrosidase in complex with cyclophellitol activity based probe with Cy5 tag (ME569) [Homo sapiens],6Q6K_B Crystal structure of recombinant human beta-glucocerebrosidase in complex with cyclophellitol activity based probe with Cy5 tag (ME569) [Homo sapiens],6Q6L_A Crystal structure of recombinant human beta-glucocerebrosidase in complex with adamantyl-cyclophellitol inhibitor (ME656) [Homo sapiens],6Q6L_B Crystal structure of recombinant human beta-glucocerebrosidase in complex with adamantyl-cyclophellitol inhibitor (ME656) [Homo sapiens],6Q6N_A Crystal structure of recombinant human beta-glucocerebrosidase in complex with biphenyl-cyclophellitol inhibitor (ME655) [Homo sapiens],6Q6N_B Crystal structure of recombinant human beta-glucocerebrosidase in complex with biphenyl-cyclophellitol inhibitor (ME655) [Homo sapiens],6TJJ_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6TJJ_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6YTP_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6YTP_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6YUT_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6YUT_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6YV3_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6YV3_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6Z39_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6Z39_BBB Chain BBB, Glucosylceramidase [Homo sapiens]
2WKL_A 6.50e-54 35 411 66 463
Velaglucerasealfa [Homo sapiens],2WKL_B Velaglucerase alfa [Homo sapiens],5LVX_A Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator [Homo sapiens],5LVX_B Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator [Homo sapiens],5LVX_C Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator [Homo sapiens],5LVX_D Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator [Homo sapiens],6TJK_AAA Chain AAA, Lysosomal acid glucosylceramidase [Homo sapiens],6TJK_BBB Chain BBB, Lysosomal acid glucosylceramidase [Homo sapiens],6TJQ_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6TN1_AAA Chain AAA, Lysosomal acid glucosylceramidase [Homo sapiens],6YTR_AAA Chain AAA, Lysosomal acid glucosylceramidase [Homo sapiens],6YTR_BBB Chain BBB, Lysosomal acid glucosylceramidase [Homo sapiens],6Z3I_BBB Chain BBB, Lysosomal acid glucosylceramidase [Homo sapiens],7NWV_AAA Chain AAA, Lysosomal acid glucosylceramidase [Homo sapiens],7NWV_BBB Chain BBB, Lysosomal acid glucosylceramidase [Homo sapiens]
2V3D_A 7.62e-54 35 411 68 465
acid-beta-glucosidasewith N-butyl-deoxynojirimycin [Homo sapiens],2V3D_B acid-beta-glucosidase with N-butyl-deoxynojirimycin [Homo sapiens],2V3E_A acid-beta-glucosidase with N-nonyl-deoxynojirimycin [Homo sapiens],2V3E_B acid-beta-glucosidase with N-nonyl-deoxynojirimycin [Homo sapiens],2V3F_A acid-beta-glucosidase produced in carrot [Homo sapiens],2V3F_B acid-beta-glucosidase produced in carrot [Homo sapiens],2VT0_A X-ray structure of a conjugate with conduritol-beta-epoxide of acid-beta-glucosidase overexpressed in cultured plant cells [Homo sapiens],2VT0_B X-ray structure of a conjugate with conduritol-beta-epoxide of acid-beta-glucosidase overexpressed in cultured plant cells [Homo sapiens],2WCG_A X-ray structure of acid-beta-glucosidase with N-octyl(cyclic guanidine)-nojirimycin in the active site [Homo sapiens],2WCG_B X-ray structure of acid-beta-glucosidase with N-octyl(cyclic guanidine)-nojirimycin in the active site [Homo sapiens],2XWD_A X-Ray Structure Of Acid-Beta-Glucosidase With 5n,6o-(N'-(N- Octyl)imino)nojirimycin In The Active Site [Homo sapiens],2XWD_B X-Ray Structure Of Acid-Beta-Glucosidase With 5n,6o-(N'-(N- Octyl)imino)nojirimycin In The Active Site [Homo sapiens],2XWE_A X-ray Structure Of Acid-beta-glucosidase With 5n,6s-(n'-(n- Octyl)imino)-6-thionojirimycin In The Active Site [Homo sapiens],2XWE_B X-ray Structure Of Acid-beta-glucosidase With 5n,6s-(n'-(n- Octyl)imino)-6-thionojirimycin In The Active Site [Homo sapiens]
3KE0_A 9.07e-54 35 411 66 463
ChainA, Glucosylceramidase [Homo sapiens],3KE0_B Chain B, Glucosylceramidase [Homo sapiens],3KEH_A Chain A, Glucocerebrosidase [Homo sapiens],3KEH_B Chain B, Glucocerebrosidase [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P17439 3.29e-57 35 411 85 481
Lysosomal acid glucosylceramidase OS=Mus musculus OX=10090 GN=Gba PE=1 SV=1
G5ECR8 1.54e-53 33 396 90 469
Putative glucosylceramidase 3 OS=Caenorhabditis elegans OX=6239 GN=gba-3 PE=3 SV=1
P04062 7.53e-53 35 411 105 502
Lysosomal acid glucosylceramidase OS=Homo sapiens OX=9606 GN=GBA PE=1 SV=3
Q9BDT0 7.53e-53 35 411 105 502
Lysosomal acid glucosylceramidase OS=Pan troglodytes OX=9598 GN=GBA PE=3 SV=1
Q5R8E3 1.05e-52 35 411 105 502
Lysosomal acid glucosylceramidase OS=Pongo abelii OX=9601 GN=GBA PE=2 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
0.999896 0.000154 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000423_00125.