CAZyme Information: CAGL0D06490g-T-p1

Basic Information

• Species: [Candida] glabrata
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; [Candida] glabrata
• CAZyme ID: CAGL0D06490g-T-p1
• CAZy Family: GH16
• CAZyme Description: Ortholog(s) have chitin deacetylase activity and role in ascospore wall assembly

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
354	ChrD_C_glabrata_CBS138|CGC1	40548.74	7.4533

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CglabrataCBS138	5615	284593	322	5293

• Gene Location: location=ChrD_C_glabrata_CBS138:616117-617181(+)

Full Sequence      

MCAKNMLCSYLLCNFSFGFHLCLRHAAYTSTVVFHVKIKLYSFHAMLINKMRELLVYKLL
VLTTISNLTKIVTAYSVLNKMNTELEQQFSKAPFPEWLAQFTQLQDWPGMDPPYIPLDFI
DFSKIPEATHYNQLQCETVPRDICSFDCHKCVATDDILSCDSLTQTFDDGPTPATTDLLG
NLNHKATFFTLGINIINYPQIYKAIIQRGHDVASHTWSHAHLPSLSNEKIIAQLQWSIWA
MNATGNHIPRYFRPPFGGMDNRVRAIARQFGLQAVLWDRDSFDWQLLTPNPKTEEDILKD
VCLWKKHDGRGIILEHDTTKQTTDLAIKIERIIGLSQKTVAQCVGGSNYIRQFQ

Enzyme Prediction     

EC	3.5.1.41:8

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	164	275	5.6e-24	0.8692307692307693

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200576	CE4_MrCDA_like	2.64e-69	161	329	1	173	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	4.84e-48	166	333	6	167	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	3.01e-40	166	322	13	175	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	1.07e-39	158	275	4	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.
223798	CDA1	2.41e-37	95	333	3	240	Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHS65325.1|CE4	1.59e-268	1	354	1	354
CAG58598.1|CE4	1.59e-268	1	354	1	354
QNG13039.1|CE4	2.16e-268	1	354	9	362
UCS35359.1|CE4	1.25e-267	1	354	9	362
UCS19668.1|CE4	1.25e-267	1	354	9	362

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7BLY_A	4.48e-23	166	345	45	228	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
6H8L_A	1.71e-21	166	329	15	172	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]
7FBW_A	4.87e-21	166	322	122	275	Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
5LFZ_A	3.92e-20	166	349	30	209	T48 deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
2CC0_A	2.84e-19	166	322	10	161	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q06703|CDA2_YEAST	1.60e-128	85	353	42	310	Chitin deacetylase 2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=CDA2 PE=1 SV=1
sp|Q06702|CDA1_YEAST	7.42e-117	91	353	38	300	Chitin deacetylase 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=CDA1 PE=1 SV=1
sp|J9VPD7|CDA1_CRYNH	2.02e-31	120	327	112	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|P0CP76|CDA3_CRYNJ	4.41e-30	142	286	103	256	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	6.09e-30	142	286	103	256	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
0.998281	0.001730

TMHMM  Annotations     

There is no transmembrane helices in CAGL0D06490g-T-p1.