CAZyme Information: KIS67010.1

Basic Information

• Species: Ustilago maydis
• Lineage: Basidiomycota; Ustilaginomycetes; ; Ustilaginaceae; Ustilago; Ustilago maydis
• CAZyme ID: KIS67010.1
• CAZy Family: CE8
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
462	CM003155|CGC2	50383.01	6.1340

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Umaydis521	6910	237631	145	6765

• Gene Location: location=CM003155:532565-534067(-)

Full Sequence      

MLVSKGKEFFHQSIHDNVRRAAARDGVELFALDKRQSAPHGTTEKTASQLNDPGAECAPY
SLPIINQITNQFPAVWELADILPGDIEALHLLQTIKASGVIPCGIGVRGTQPASLSGANL
DGDYNLAQDPDCWWTDNGCTEPKHAGLLPDIITCNEPYTWGYTFDDGPNCTHNALYDMWA
ANNQKASLMYIGSNVMDWPLEAQRGIVDEHHICVHTWSHRYMKALTNSQAFAELWYTIKT
IKYVMGVTRTCWRPPYGDIDDRIRGIAQGLGLRTIMWNVDTNDWNIAPPIRALFRWPQRG
IIVLEHELEQSAMNMSIEQYPAVKAAWKHVVPLTACLNITRPYPEDIFYPNFSEYIQGNV
VASGLPDASMGISSTAQVSAQGTLSGMGGSFATASDGSGNRQASPVHTAPPTGSSTKPAF
PTTISKQQSHKSSGACGTSSISVFPLVLVAVATVMGSLLACF

Enzyme Prediction     

EC	3.5.1.41:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	162	274	9.6e-19	0.8538461538461538

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200576	CE4_MrCDA_like	1.35e-70	159	324	2	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	2.66e-33	163	306	6	153	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.
200575	CE4_ClCDA_like	9.25e-28	151	311	1	174	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.
396211	Polysacc_deac_1	5.02e-26	163	275	12	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.
200578	CE4_CtAXE_like	2.58e-24	163	311	6	155	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBQ69654.1|CE4	4.30e-235	5	459	34	525
CDU23466.1|CE4	3.73e-230	5	459	34	520
SAM82034.1|CE4	1.34e-132	17	369	34	406
CBQ73077.1|CE4	3.81e-132	39	369	62	406
CDU22706.1|CE4	5.93e-132	24	369	40	406

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7FBW_A	2.59e-15	163	313	122	276	Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
2C1G_A	1.21e-14	143	349	221	427	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) [Streptococcus pneumoniae R6]
2C1I_A	5.10e-14	143	349	221	427	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) D 275 N Mutant. [Streptococcus pneumoniae R6]
2CC0_A	2.84e-13	161	307	8	156	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]
5NC6_A	2.01e-10	163	284	6	130	Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (E)-N-hydroxy-3-(naphthalen-1-yl)prop-2-enamide [Bacillus cereus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VND2|CDA2_CRYNH	7.57e-94	42	358	44	374	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
sp|Q55U20|CDA2_CRYNB	1.17e-93	42	358	45	375	Chitin deacetylase 2 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=CDA2 PE=1 SV=1
sp|P50325|CDA_AMYRO	5.40e-81	52	363	52	376	Chitin deacetylase OS=Amylomyces rouxii OX=29923 GN=CDA PE=1 SV=1
sp|J9VPD7|CDA1_CRYNH	2.39e-36	123	317	130	342	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|P0CP77|CDA3_CRYNB	1.74e-31	139	327	105	311	Chitin deacetylase 3 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=CDA3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000027	0.000037

TMHMM  Annotations     

There is no transmembrane helices in KIS67010.1.