CAZyme Information: sr12442-t26_1-p1

Basic Information

• Species: Sporisorium reilianum
• Lineage: Basidiomycota; Ustilaginomycetes; ; Ustilaginaceae; Sporisorium; Sporisorium reilianum
• CAZyme ID: sr12442-t26_1-p1
• CAZy Family: GH16
• CAZyme Description: related to chitin deacetylase precursor

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
478		50472.39	7.0968

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SreilianumSRZ2	6791	999809	118	6673

• Gene Location: location=FQ311441:975341-976777(+)

Full Sequence      

MRLTTLTVGAMALAAPLVAASGYHERGLVDPKHHPAGHLFHKRADEHHSLTKRQLATTSK
NGMPYPPAGSDPPPASSLPKAWIDRYNAKKAAGLIPDIPRSITDPNTRATTYPAGTDMTN
VCSWTVQKCDTGDIWLAPDNYVAVTFDDGPTPQSPDLINYLQSQGTSATHFLIGSAIVWN
PTAMDQYVKADPPMHLGVHTWSHTLQTGKTDLEILGDLGWTMQIIYDLTGSVPMYWRPPE
GDVDARVRAIATQVLGLQTVMWNKDADDWCLRQGNGTAQLTTCTTGIGASKQSVIREMTS
WANTNNRTGFISLEHETTDQAIDSFKSYLRALKRNNWNVGAVPELQGLPYYQNQWNLTSK
KEAVDSILPTRQPINVVNSDAPRGSARAPDTSAFANLDGSGASASASSAASAAVASSSAA
RPLASSTSGSTSSSGSSGSSTSSSAATKGASTSGASSLIAGASTVGLGVVAAVFALML

Enzyme Prediction     

No EC number prediction in sr12442-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	138	253	3.4e-18	0.8615384615384616

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200576	CE4_MrCDA_like	2.28e-77	140	332	1	178	Catalytic NodB homology domain of Mucor rouxii chitin deacetylase and similar proteins. This family is represented by the chitin deacetylase (MrCDA, EC 3.5.1.41) encoded from the fungus Mucor rouxii (also known as Amylomyces rouxii). MrCDA is an acidic glycoprotein with a very stringent specificity for beta1-4-linked N-acetylglucosamine homopolymers. It requires at least four residues (chitotetraose) for catalysis, and can achieve extensive deacetylation on chitin polymers. MrCDA shows high sequence similarity to Colletotrichum lindemuthianum chitin deacetylase (endo-chitin de-N-acetylase, ClCDA), which consists of a single catalytic domain similar to the deformed (beta/alpha)8 barrel fold adopted by the carbohydrate esterase 4 (CE4) superfamily, 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. The family also includes some uncharacterized eukaryotic and bacterial homologs of MrCDA.
213022	CE4_NodB_like_6s_7s	3.02e-28	140	333	1	171	Catalytic NodB homology domain of rhizobial NodB-like proteins. This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ 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. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal.
396211	Polysacc_deac_1	3.20e-23	138	260	5	124	Polysaccharide deacetylase. This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyzes glucosidic bonds in xylan.
200571	CE4_SpPgdA_BsYjeA_like	7.67e-22	141	269	2	125	Catalytic NodB homology domain of Streptococcus pneumoniae peptidoglycan deacetylase PgdA, Bacillus subtilis BsYjeA protein, and their bacterial homologs. This family is represented by Streptococcus pneumoniae peptidoglycan GlcNAc deacetylase (SpPgdA), a member of the carbohydrate esterase 4 (CE4) superfamily. SpPgdA protects gram-positive bacterial cell wall from host lysozymes by deacetylating peptidoglycan N-acetylglucosamine (GlcNAc) residues. It consists of three separate domains: N-terminal, middle and C-terminal (catalytic) domains. The catalytic NodB homology domain is similar to the deformed (beta/alpha)8 barrel fold adopted by other CE4 esterases, which harbors a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The enzyme is able to accept GlcNAc3 as a substrate, with the N-acetyl of the middle sugar being removed by the enzyme. This family also includes Bacillus subtilis BsYjeA protein encoded by the yjeA gene, which is one of the six polysaccharide deacetylase gene homologs (pdaA, pdaB/ybaN, yheN, yjeA, yxkH and ylxY) in the Bacillus subtilis genome. Although homology comparison shows that the BsYjeA protein contains a polysaccharide deacetylase domain, and was predicted to be a membrane-bound xylanase or a membrane-bound chitooligosaccharide deacetylase, more recent research indicates BsYjeA might be a novel non-specific secretory endonuclease which creates random nicks progressively on the two strands of dsDNA, resulting in highly distinguishable intermediates/products very different in chemical and physical compositions over time. In addition, BsYjeA shares several enzymatic properties with the well-understood DNase I endonuclease. Both enzymes are active on ssDNA and dsDNA, both generate random nicks, and both require Mg2+ or Mn2+ for hydrolytic activity.
200577	CE4_SlAXE_like	6.95e-21	141	305	2	159	Catalytic NodB homology domain of Streptomyces lividans acetylxylan esterase and its bacterial homologs. This family is represented by Streptomyces lividans acetylxylan esterase (SlAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. SlAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan as a result of deacetylation. SlAXE also functions as a chitin and chitooligosaccharide de-N-acetylase with equal efficiency to its activity on xylan. SlAXE forms a dimer. Each monomer contains a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as 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. SlAXE possess a single metal center with a chemical preference for Co2+.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBQ70546.1|CE4	2.91e-311	1	478	1	478
SJX61220.1|CE4	1.31e-307	1	478	1	487
CDU24419.1|CE4	7.65e-286	1	478	1	477
SAM77146.1|CE4	3.66e-271	1	404	1	403
CDI52077.1|CE4	1.00e-267	1	478	1	477

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2CC0_A	6.48e-16	137	269	2	131	Family 4 carbohydrate esterase from Streptomyces lividans in complex with acetate [Streptomyces lividans],2CC0_B Family 4 carbohydrate esterase from Streptomyces lividans in complex with acetate [Streptomyces lividans]
7BLY_A	2.32e-11	140	360	40	239	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
5LFZ_A	8.30e-11	142	269	27	148	T48 deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
2Y8U_A	6.06e-09	126	239	17	130	Chain A, CHITIN DEACETYLASE [Aspergillus nidulans],2Y8U_B Chain B, CHITIN DEACETYLASE [Aspergillus nidulans]
7AX7_A	2.15e-08	139	239	3	102	Crystal structure of the Xyl-CE4 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides [uncultured bacterium]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P82476|CDA3_CRYNH	1.60e-54	6	353	5	327	Chitin deacetylase 3 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CDA3 PE=1 SV=3
sp|P0CP77|CDA3_CRYNB	6.78e-49	6	353	5	327	Chitin deacetylase 3 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=CDA3 PE=3 SV=1
sp|P0CP76|CDA3_CRYNJ	4.96e-48	1	353	5	327	Chitin deacetylase 3 OS=Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) OX=214684 GN=CDA3 PE=2 SV=1
sp|J9VPD7|CDA1_CRYNH	4.30e-36	55	329	81	345	Chitin deacetylase 1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CDA1 PE=1 SV=1
sp|P50325|CDA_AMYRO	1.63e-27	106	334	117	342	Chitin deacetylase OS=Amylomyces rouxii OX=29923 GN=CDA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000858	0.999101	CS pos: 20-21. Pr: 0.9434

TMHMM  Annotations     

Start	End
454	476