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CAZyme Information: OJD15366.1

You are here: Home > Sequence: OJD15366.1

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 Emergomyces pasteurianus
Lineage Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Emergomyces; Emergomyces pasteurianus
CAZyme ID OJD15366.1
CAZy Family GH47
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
684 75632.80 8.4606
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_EpasteurianusEp9510 9078 1447872 128 8950
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.52:4

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH3 97 287 2.9e-16 0.8425925925925926

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395747 Glyco_hydro_3 3.68e-17 10 324 6 313
Glycosyl hydrolase family 3 N terminal domain.
395465 Acetyltransf_1 2.06e-09 383 465 1 89
Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.
224167 ArgA 7.24e-08 607 676 56 135
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism].
173926 NAT_SF 1.06e-07 415 465 4 55
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate. NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.
404402 Acetyltransf_7 2.28e-06 408 465 1 57
Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.84e-186 1 682 1 848
1.41e-107 1 676 1 848
1.05e-106 6 676 6 848
2.05e-99 6 676 6 850
2.27e-99 1 680 1 857

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.91e-49 2 676 5 854
A unique GCN5-related glucosamine N-acetyltransferase region exist in the fungal multi-domain GH3 beta-N-acetylglucosaminidase [Rhizomucor miehei CAU432],4ZM6_B A unique GCN5-related glucosamine N-acetyltransferase region exist in the fungal multi-domain GH3 beta-N-acetylglucosaminidase [Rhizomucor miehei CAU432]
1.79e-24 6 328 13 337
Structure of a glycoside hydrolase family 3 beta-N-acetylglucosaminidase from Paenibacillus sp. str. FPU-7 [Paenibacillaceae]
1.67e-11 39 329 28 311
Chain A, Beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],7VI6_B Chain B, Beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],7VI7_A Chain A, Beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],7VI7_B Chain B, Beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835]
2.02e-07 117 333 99 314
Crystal structure of CbsA from Thermotoga neapolitana [Thermotoga neapolitana],5BZA_B Crystal structure of CbsA from Thermotoga neapolitana [Thermotoga neapolitana],5BZA_C Crystal structure of CbsA from Thermotoga neapolitana [Thermotoga neapolitana],5BZA_D Crystal structure of CbsA from Thermotoga neapolitana [Thermotoga neapolitana],5C0Q_A Crystal structure of Zn bound CbsA from Thermotoga neapolitana [Thermotoga neapolitana],5C0Q_B Crystal structure of Zn bound CbsA from Thermotoga neapolitana [Thermotoga neapolitana],5C0Q_C Crystal structure of Zn bound CbsA from Thermotoga neapolitana [Thermotoga neapolitana],5C0Q_D Crystal structure of Zn bound CbsA from Thermotoga neapolitana [Thermotoga neapolitana]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.06e-07 421 670 62 294
Mycothiol acetyltransferase OS=Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101) OX=471857 GN=mshD PE=3 SV=1
9.17e-06 607 670 350 413
Amino-acid acetyltransferase OS=Edwardsiella ictaluri (strain 93-146) OX=634503 GN=argA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000051 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in OJD15366.1.