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CAZyme Information: MGYG000000675_00078

You are here: Home > Sequence: MGYG000000675_00078

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 Bacteroides congonensis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides congonensis
CAZyme ID MGYG000000675_00078
CAZy Family GH30
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
491 MGYG000000675_1|CGC4 56688.64 8.0512
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000675 5782172 MAG Kazakhstan Asia
Gene Location Start: 104232;  End: 105707  Strand: -

Full Sequence      Download help

MNLKKLCTLG  TLLAFFSSIY  AQSFIWISST  DNNVWKEAKI  RLQADSQNIP  LLSVDGTENI60
QIFKKWGTCF  NELGWDALNM  LPLKEQDAVL  NNLFSPDGDL  RFSMGRIPMN  ANDYARNWYS120
CDEVPGDFRL  KYFNINRDKT  TLIPYIKRVQ  RINSDMTFWA  SPWSPPSWMK  VNHYYSVRSK180
AEVNQLPVKH  EIALYEGADN  VDKTFYPKQV  AVNDYFIQDT  RYLQAYANYF  CKFVSAYQEE240
GVTISRVMFQ  NEPWAYSIYP  ACAWTPEGII  RFNVEYFAPT  IKKLHPDVQV  YLGTLNTNRI300
ELVEKVLSDP  RMKDAVEGVG  FQWWGGQILP  EIRKKYPNYK  YMQTESECGS  GTFDWKAAEH360
TFNLISHYLG  NGCEEYTFWN  AILCDAGTSG  WGWKQNALIR  VDSKTASVTY  TPEYYAVKHF420
SNKVVSGTKV  LQYKAKGEDK  LPVVIFLTPE  KRYLVVAANF  NDEPKNLTVK  LGDKFLDVTL480
KAHSFNTFSM  K491

Enzyme Prediction      help

No EC number prediction in MGYG000000675_00078.

CAZyme Signature Domains help

Created with Snap2449739812214717119622024527029431934336839241744146653488GH30
Family Start End Evalue family coverage
GH30 53 488 1.2e-179 0.9904076738609112

CDD Domains      download full data without filtering help

Created with Snap2449739812214717119622024527029431934336839241744146664421Glyco_hydro_3050488XynC
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02055 Glyco_hydro_30 3.98e-37 64 421 2 345
Glycosyl hydrolase family 30 TIM-barrel domain.
COG5520 XynC 3.53e-29 50 488 34 426
O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Created with Snap2449739812214717119622024527029431934336839241744146619491QIU97424.1|GH30_23491AVM53962.1|GH30_23491BAR52714.1|GH30_23491BAR49889.1|GH30_24491AEW22095.1|GH30_2
Hit ID E-Value Query Start Query End Hit Start Hit End
QIU97424.1 8.55e-303 19 491 1 473
AVM53962.1 2.15e-287 3 491 5 493
BAR52714.1 5.88e-285 3 491 5 493
BAR49889.1 4.81e-284 3 491 5 493
AEW22095.1 6.84e-284 4 491 6 493

PDB Hits      download full data without filtering help

Created with Snap24497398122147171196220245270294319343368392417441466514881OGS_A514882WKL_A514882V3D_A514886T13_A514872WNW_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
1OGS_A 2.58e-27 51 488 66 492
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 2.58e-27 51 488 66 492
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 2.75e-27 51 488 68 494
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]
6T13_A 3.43e-27 51 488 105 531
ChainA, Glucosylceramidase [Homo sapiens],6T13_B Chain B, Glucosylceramidase [Homo sapiens],6T13_C Chain C, Glucosylceramidase [Homo sapiens],6T13_D Chain D, Glucosylceramidase [Homo sapiens]
2WNW_A 3.99e-27 51 487 33 439
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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap2449739812214717119622024527029431934336839241744146622437sp|G5ECR8|GLCM3_CAEEL51488sp|P17439|GLCM_MOUSE52459sp|O16580|GLCM1_CAEEL51488sp|Q70KH2|GLCM_PIG51488sp|P04062|GLCM_HUMAN
Hit ID E-Value Query Start Query End Hit Start Hit End Description
G5ECR8 1.03e-30 22 437 59 463
Putative glucosylceramidase 3 OS=Caenorhabditis elegans OX=6239 GN=gba-3 PE=3 SV=1
P17439 2.81e-29 51 488 85 510
Lysosomal acid glucosylceramidase OS=Mus musculus OX=10090 GN=Gba PE=1 SV=1
O16580 2.53e-28 52 459 87 481
Putative glucosylceramidase 1 OS=Caenorhabditis elegans OX=6239 GN=gba-1 PE=1 SV=2
Q70KH2 1.71e-27 51 488 105 531
Lysosomal acid glucosylceramidase OS=Sus scrofa OX=9823 GN=GBA PE=3 SV=1
P04062 1.88e-26 51 488 105 531
Lysosomal acid glucosylceramidase OS=Homo sapiens OX=9606 GN=GBA PE=1 SV=3

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
0.000646 0.998553 0.000180 0.000217 0.000182 0.000178

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000675_00078.