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CAZyme Information: EDK43323.1

You are here: Home > Sequence: EDK43323.1

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 Lodderomyces elongisporus
Lineage Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Lodderomyces; Lodderomyces elongisporus
CAZyme ID EDK43323.1
CAZy Family GH16
CAZyme Description glucan 1,3-beta-glucosidase precursor
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
427 CH981525|CGC17 48814.14 4.3860
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_LelongisporusNRRLYB-4239 5908 379508 109 5799
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.58:29 3.2.1.21:6 3.2.1.75:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 104 394 1.1e-125 0.9966996699669967

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
225344 BglC 8.79e-79 54 424 19 395
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098 Cellulase 7.78e-08 109 260 24 165
Cellulase (glycosyl hydrolase family 5).
396011 AP_endonuc_2 0.001 121 225 79 179
Xylose isomerase-like TIM barrel. This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.
277321 MPP_ASMase 0.004 102 222 141 251
acid sphingomyelinase and related proteins, metallophosphatase domain. Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.14e-236 6 425 4 421
3.39e-235 7 427 5 423
1.03e-226 36 426 24 431
1.08e-225 36 426 31 438
1.08e-225 36 426 31 438

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.13e-227 45 426 1 394
Exo-b-(1,3)-glucanase From Candida Albicans At 1.85 A Resolution [Candida albicans],1EQC_A Exo-b-(1,3)-glucanase From Candida Albicans In Complex With Castanospermine At 1.85 A [Candida albicans]
2.66e-227 45 426 7 400
Exo-B-(1,3)-Glucanase from Candida Albicans in complex with unhydrolysed and covalently linked 2,4-dinitrophenyl-2-deoxy-2-fluoro-B-D-glucopyranoside at 1.9 A [Candida albicans]
7.62e-227 45 426 7 400
Chain A, Hypothetical protein XOG1 [Candida albicans]
7.62e-227 45 426 7 400
Chain A, Hypothetical protein XOG1 [Candida albicans]
1.48e-226 45 426 6 399
The structure of E292S glycosynthase variant of exo-1,3-beta-glucanase from Candida albicans at 1.85A resolution [Candida albicans SC5314],4M81_A The structure of E292S glycosynthase variant of exo-1,3-beta-glucanase from Candida albicans complexed with 1-fluoro-alpha-D-glucopyranoside (donor) and p-nitrophenyl beta-D-glucopyranoside (acceptor) at 1.86A resolution [Candida albicans SC5314],4M82_A The structure of E292S glycosynthase variant of exo-1,3-beta-glucanase from Candida albicans complexed with p-nitrophenyl-gentiobioside (product) at 1.6A resolution [Candida albicans SC5314]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.88e-226 36 426 31 438
Glucan 1,3-beta-glucosidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=XOG1 PE=1 SV=5
9.20e-210 31 425 19 425
Glucan 1,3-beta-glucosidase OS=Schwanniomyces occidentalis OX=27300 PE=3 SV=1
3.68e-202 39 425 23 425
Glucan 1,3-beta-glucosidase OS=Candida oleophila OX=45573 GN=EXG1 PE=3 SV=1
1.36e-195 46 424 35 427
Glucan 1,3-beta-glucosidase 2 OS=Wickerhamomyces anomalus OX=4927 GN=EXG2 PE=3 SV=1
9.20e-180 40 425 35 439
Glucan 1,3-beta-glucosidase OS=Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651) OX=226302 GN=EXG1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000467 0.999514 CS pos: 23-24. Pr: 0.6736

TMHMM  Annotations      help

There is no transmembrane helices in EDK43323.1.