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CAZyme Information: EPrPAT00000020218-p1

You are here: Home > Sequence: EPrPAT00000020218-p1

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 Pythium aphanidermatum
Lineage Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum
CAZyme ID EPrPAT00000020218-p1
CAZy Family GH7
CAZyme Description Glucan 1,3-beta-glucosidase.
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1118 123425.83 4.9352
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PaphanidermatumDAOMBR444 12363 1223555 58 12305
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC - -

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 160 437 4.1e-169 0.9964028776978417
CBM43 575 647 9.2e-16 0.9156626506024096

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
240619 SAHH 0.0 752 1105 1 401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains. S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.
235488 PRK05476 0.0 736 1112 1 425
S-adenosyl-L-homocysteine hydrolase; Provisional
240258 PTZ00075 0.0 742 1118 4 476
Adenosylhomocysteinase; Provisional
178111 PLN02494 0.0 738 1118 1 477
adenosylhomocysteinase
398750 AdoHcyase 0.0 742 1117 1 461
S-adenosyl-L-homocysteine hydrolase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 56 692 62 707
0.0 58 649 43 636
0.0 58 705 41 678
0.0 56 649 28 627
0.0 59 704 86 730

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.28e-163 736 1118 10 488
Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine [Lupinus luteus],3OND_B Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine [Lupinus luteus],3ONE_A Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenine [Lupinus luteus],3ONE_B Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenine [Lupinus luteus],3ONF_A Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with cordycepin [Lupinus luteus],3ONF_B Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with cordycepin [Lupinus luteus]
4.71e-146 743 1118 24 485
Crystal Structure of S-adenosyl-L-homocysteine hydrolase from Acanthamoeba castellanii with bound NAD and Adenosine [Acanthamoeba castellanii str. Neff],6UK3_B Crystal Structure of S-adenosyl-L-homocysteine hydrolase from Acanthamoeba castellanii with bound NAD and Adenosine [Acanthamoeba castellanii str. Neff],6UK3_C Crystal Structure of S-adenosyl-L-homocysteine hydrolase from Acanthamoeba castellanii with bound NAD and Adenosine [Acanthamoeba castellanii str. Neff],6UK3_D Crystal Structure of S-adenosyl-L-homocysteine hydrolase from Acanthamoeba castellanii with bound NAD and Adenosine [Acanthamoeba castellanii str. Neff]
3.48e-135 739 1118 31 494
Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],3D64_B Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],3GLQ_A Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei in complex with 9-beta-D-arabino-furansyl-adenine [Burkholderia pseudomallei 1710b],3GLQ_B Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei in complex with 9-beta-D-arabino-furansyl-adenine [Burkholderia pseudomallei 1710b]
2.13e-132 742 1118 19 494
Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and adenosine [Mycobacterium tuberculosis H37Rv],3CE6_B Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and adenosine [Mycobacterium tuberculosis H37Rv],3CE6_C Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and adenosine [Mycobacterium tuberculosis H37Rv],3CE6_D Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and adenosine [Mycobacterium tuberculosis H37Rv]
2.20e-132 742 1118 20 495
Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 3-deazaadenosine [Mycobacterium tuberculosis H37Rv],2ZIZ_B Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 3-deazaadenosine [Mycobacterium tuberculosis H37Rv],2ZIZ_C Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 3-deazaadenosine [Mycobacterium tuberculosis H37Rv],2ZIZ_D Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 3-deazaadenosine [Mycobacterium tuberculosis H37Rv],2ZJ0_A Crystal structure of Mycobacterium tuberculosis S-Adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 2-fluoroadenosine [Mycobacterium tuberculosis H37Rv],2ZJ0_B Crystal structure of Mycobacterium tuberculosis S-Adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 2-fluoroadenosine [Mycobacterium tuberculosis H37Rv],2ZJ0_C Crystal structure of Mycobacterium tuberculosis S-Adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 2-fluoroadenosine [Mycobacterium tuberculosis H37Rv],2ZJ0_D Crystal structure of Mycobacterium tuberculosis S-Adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 2-fluoroadenosine [Mycobacterium tuberculosis H37Rv],2ZJ1_A Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 3'-keto-aristeromycin [Mycobacterium tuberculosis H37Rv],2ZJ1_B Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 3'-keto-aristeromycin [Mycobacterium tuberculosis H37Rv],2ZJ1_C Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 3'-keto-aristeromycin [Mycobacterium tuberculosis H37Rv],2ZJ1_D Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 3'-keto-aristeromycin [Mycobacterium tuberculosis H37Rv],3DHY_A Chain A, Adenosylhomocysteinase [Mycobacterium tuberculosis],3DHY_B Chain B, Adenosylhomocysteinase [Mycobacterium tuberculosis],3DHY_C Chain C, Adenosylhomocysteinase [Mycobacterium tuberculosis],3DHY_D Chain D, Adenosylhomocysteinase [Mycobacterium tuberculosis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.20e-167 736 1118 7 485
Adenosylhomocysteinase OS=Mesembryanthemum crystallinum OX=3544 GN=SAHH PE=2 SV=1
4.97e-165 736 1118 7 485
Adenosylhomocysteinase OS=Nicotiana sylvestris OX=4096 GN=SAHH PE=2 SV=1
4.97e-165 736 1118 7 485
Adenosylhomocysteinase OS=Nicotiana tabacum OX=4097 GN=SAHH PE=2 SV=1
1.95e-164 736 1118 7 485
Adenosylhomocysteinase OS=Phalaenopsis sp. OX=36900 GN=SAHH PE=2 SV=1
2.75e-164 736 1118 7 485
Adenosylhomocysteinase OS=Catharanthus roseus OX=4058 GN=SAHH PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000608 0.999366 CS pos: 20-21. Pr: 0.9746

TMHMM  Annotations      help

There is no transmembrane helices in EPrPAT00000020218-p1.