logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: POW07923.1

You are here: Home > Sequence: POW07923.1

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 Puccinia striiformis
Lineage Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis
CAZyme ID POW07923.1
CAZy Family GH18
CAZyme Description Chitin deacetylase [Source:UniProtKB/TrEMBL;Acc:A0A2S4VEH6]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1214 135460.18 9.4553
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Pstriiformis93TX-2 14629 N/A 0 14629
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.1.1.72:1 3.5.1.41:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE4 40 165 5e-29 0.9153846153846154
CE4 998 1112 1.7e-20 0.9153846153846154

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
341237 Firefly_Luc_like 1.06e-99 364 947 37 486
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL). This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
223395 CaiC 2.08e-77 364 829 65 472
Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism].
341230 4CL 1.62e-76 364 951 59 505
4-Coumarate-CoA Ligase (4CL). 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
200575 CE4_ClCDA_like 4.13e-70 36 230 1 197
Catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase and similar proteins. This family is represented by the chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41) from Colletotrichum lindemuthianum (also known as Glomerella lindemuthiana), which is a member of the carbohydrate esterase 4 (CE4) superfamily. ClCDA catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. It consists of a single catalytic domain similar to the deformed (alpha/beta)8 barrel fold adopted by other CE4 esterases, which encompasses a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine), to carry out acid/base catalysis. It possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite affinity. Unlike its bacterial homologs, ClCDA contains two intramolecular disulfide bonds that may add stability to this secreted protein. The family also includes many uncharacterized deacetylases and hypothetical proteins mainly from eukaryotes, which show high sequence similarity to ClCDA.
341228 AFD_class_I 3.83e-66 508 843 1 310
Adenylate forming domain, Class I, also known as the ANL superfamily. This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.48e-97 37 254 38 255
2.20e-67 35 254 54 269
1.71e-57 8 254 13 251
8.80e-57 967 1206 11 248
4.14e-56 967 1206 11 248

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.91e-48 509 828 183 483
Crystal structure of 4-coumarate:CoA ligase delta-V341 mutant complexed with feruloyl adenylate [Nicotiana tabacum],5BSW_B Crystal structure of 4-coumarate:CoA ligase delta-V341 mutant complexed with feruloyl adenylate [Nicotiana tabacum]
2.86e-47 509 828 183 484
Crystal structure of 4-coumarate:CoA ligase complexed with magnesium and Adenosine triphosphate [Nicotiana tabacum],5BSM_B Crystal structure of 4-coumarate:CoA ligase complexed with magnesium and Adenosine triphosphate [Nicotiana tabacum],5BSR_A Crystal structure of 4-coumarate:CoA ligase complexed with adenosine monophosphate and Coenzyme A [Nicotiana tabacum],5BST_A Crystal structure of 4-coumarate:CoA ligase complexed with coumaroyl adenylate [Nicotiana tabacum],5BSU_A Crystal structure of 4-coumarate:CoA ligase complexed with caffeoyl adenylate [Nicotiana tabacum],5BSV_A Crystal structure of 4-coumarate:CoA ligase complexed with feruloyl adenylate [Nicotiana tabacum]
5.20e-47 509 828 183 484
Structure of the open conformation of 4-coumarate-CoA ligase from Nicotiana tabacum [Nicotiana tabacum],5U95_B Structure of the open conformation of 4-coumarate-CoA ligase from Nicotiana tabacum [Nicotiana tabacum],5U95_C Structure of the open conformation of 4-coumarate-CoA ligase from Nicotiana tabacum [Nicotiana tabacum],5U95_D Structure of the open conformation of 4-coumarate-CoA ligase from Nicotiana tabacum [Nicotiana tabacum]
1.14e-46 509 855 180 508
Crystal structures and enzymatic mechanisms of a Populus tomentosa 4-coumarate--CoA ligase [Populus tomentosa],3A9V_A Crystal structures and enzymatic mechanisms of a Populus tomentosa 4-coumarate--CoA ligase [Populus tomentosa],3NI2_A Crystal structures and enzymatic mechanisms of a Populus tomentosa 4-coumarate:CoA ligase [Populus tomentosa]
6.06e-44 364 832 115 532
4-Coumaroyl-CoA Ligase::Stilbene Synthase fusion protein [Arabidopsis thaliana]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.24e-49 492 828 159 485
4-coumarate-CoA ligase 1 OS=Narcissus pseudonarcissus OX=39639 GN=4CL1 PE=2 SV=1
2.65e-49 364 840 90 510
4-coumarate--CoA ligase 2 OS=Arabidopsis thaliana OX=3702 GN=4CL2 PE=1 SV=2
3.92e-49 364 834 102 515
4-coumarate--CoA ligase 3 OS=Arabidopsis thaliana OX=3702 GN=4CL3 PE=1 SV=1
4.32e-48 509 828 186 487
4-coumarate--CoA ligase 1 OS=Solanum tuberosum OX=4113 GN=4CL1 PE=3 SV=1
7.71e-48 365 828 81 485
4-coumarate--CoA ligase 1 OS=Petroselinum crispum OX=4043 GN=4CL1 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.001339 0.998618 CS pos: 24-25. Pr: 0.9549

TMHMM  Annotations      help

There is no transmembrane helices in POW07923.1.