CAZyme Information: OCF67628.1

Basic Information

• Species: Kwoniella mangrovensis
• Lineage: Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella mangrovensis
• CAZyme ID: OCF67628.1
• CAZy Family: GH72
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
427		45097.71	4.2725

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_KmangroviensisCBS8507	8555	1296122	133	8422

• Gene Location: location=KI669476:775973-777649(-)

Full Sequence      

MFTHTLLSTFSFLVIAAAAAPVDESWVQPRDSPVHELFYKRAPNPSDPNFASNYPAPGST
PPTDSLPQAWTDKLKTINLPDVQPSSPNNGYPTYADGETPYDQKICSFTYQCTTDEDLYN
PPSGVLALSFDDGPGDASPDLYSFLAANNISTAATHFMIGGNIVYNPTGMQAAVDAGGLI
GVHTWSHQYTTTLSNEGVLGELGWTMQIISDLNGGRIPKYWRPPYGDVDNRVRAIAKGVF
GLETVVWNTDSADWAIGSDARYTHDSVVSQVNQWLSGNKTNGLLLLEHEIQQTEVDVFKA
IFPSIGSNGWTIKNVADAWGMDWYVNSGKTNTEAITTMSVGASTLAVTNQTTSQQSSTSA
SASASVSTTSGSASTTSAQVASSTSTSSATAAAAANSGSSSSASSTLMIPGFSLAGLGFL
TALFLQV

Enzyme Prediction     

EC	3.5.1.41:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	121	237	8.4e-18	0.8615384615384616

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200576	CE4_MrCDA_like	2.76e-71	124	306	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	1.25e-37	124	305	1	170	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.
200578	CE4_CtAXE_like	6.85e-32	127	315	4	177	Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its bacterial homologs. This family is represented by Clostridium thermocellum acetylxylan esterase (CtAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. CtAXE 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 consequence of deacetylation. CtAXE is a monomeric protein containing a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases. However, due to differences in the topography of the substrate-binding groove, the chemistry of the active center, and metal ion coordination, CtAXE has different metal ion preference and lacks activity on N-acetyl substrates. It is significantly activated by Co2+. Moreover, CtAXE displays distinctly different ligand coordination to the metal ion, utilizing an aspartate, a histidine, and four water molecules, as opposed to the conserved His-His-Asp zinc-binding triad of other CE4 esterases.
396211	Polysacc_deac_1	4.98e-30	120	237	3	117	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	5.30e-28	125	311	2	173	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UOH80811.1|CE4	1.34e-140	1	340	1	341
AUB24639.1|CE4	3.10e-139	1	340	1	341
AFR94907.1|CE4	3.10e-139	1	340	1	341
ADV21929.1|CE4	1.65e-138	1	349	1	352
AAW42893.1|CE4|3.5.1.41	3.32e-138	1	351	1	351

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2CC0_A	2.13e-19	123	309	4	176	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]
6H8L_A	2.75e-18	116	316	2	187	Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],6H8L_B Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
6H8N_A	1.78e-17	116	316	2	187	Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis - mutant D285S [Bacillus subtilis subsp. subtilis str. 168],6H8N_B Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis - mutant D285S [Bacillus subtilis subsp. subtilis str. 168]
2Y8U_A	3.80e-12	111	324	28	229	Chain A, CHITIN DEACETYLASE [Aspergillus nidulans],2Y8U_B Chain B, CHITIN DEACETYLASE [Aspergillus nidulans]
2IW0_A	9.58e-12	124	324	42	246	Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [Colletotrichum lindemuthianum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P82476|CDA3_CRYNH	5.50e-140	1	340	1	341	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|P0CP76|CDA3_CRYNJ	5.90e-139	1	351	1	351	Chitin deacetylase 3 OS=Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) OX=214684 GN=CDA3 PE=2 SV=1
sp|P0CP77|CDA3_CRYNB	8.36e-139	1	351	1	351	Chitin deacetylase 3 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=CDA3 PE=3 SV=1
sp|J9VPD7|CDA1_CRYNH	3.29e-36	52	342	89	390	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|J9VND2|CDA2_CRYNH	1.09e-32	128	307	161	340	Chitin deacetylase 2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CDA2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000858	0.999110	CS pos: 19-20. Pr: 0.9445

TMHMM  Annotations     

There is no transmembrane helices in OCF67628.1.