CAZyme Information: RO3G_01608-t26_1-p1

Basic Information

• Species: Rhizopus delemar
• Lineage: Mucoromycota; Mucoromycetes; ; Rhizopodaceae; Rhizopus; Rhizopus delemar
• CAZyme ID: RO3G_01608-t26_1-p1
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
189	CH476732|CGC7	21191.09	10.0440

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RdelemarRA99-880	17703	246409	244	17459

• Gene Location: location=CH476732:4162847-4163483(+)

Full Sequence      

MNGNNWVNVETQSVNTPAGVKTYKQVIKHVYDKGHQIASHTYSHKELGGLSAAEVKSEMT
KLDKIFKSVIGKSPLYMRPPSGSYDDNTLAALGNLGYKVILWDIDSNDWRYKDISSLSNE
QANYKSVIDKDSKKNPHGHIALQHDVHKKTVTKLVPWVISYVKSKKNYKFVSVAECLGQS
KTSAYKSSK

Enzyme Prediction     

No EC number prediction in RO3G_01608-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	20	99	6.6e-18	0.5923076923076923

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200575	CE4_ClCDA_like	1.38e-56	1	173	40	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.
213022	CE4_NodB_like_6s_7s	1.03e-38	20	163	39	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.
200578	CE4_CtAXE_like	5.66e-33	20	175	39	179	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.
274287	spore_ybaN_pdaB	1.20e-31	20	177	44	191	polysaccharide deacetylase family sporulation protein PdaB. This model describes the YbaN protein family, also called PdaB and SpoVIE, of Gram-positive bacteria. Although ybaN null mutants have only a mild sporulation defect, ybaN/ytrI double mutants show drastically reducted sporulation efficiencies. This synthetic defect suggests the role of this sigmaE-controlled gene in sporulation had been masked by functional redundancy. Members of this family are homologous to a characterized polysaccharide deacetylase; the exact function this protein family is unknown. [Cellular processes, Sporulation and germination]
223798	CDA1	1.71e-29	20	177	103	257	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
CDS05261.1|CE4	7.52e-49	1	178	71	236
QRW12840.1|CE4	3.08e-36	28	178	93	235
QRV98282.1|CE4	1.72e-35	28	178	93	235
CEI62102.1|CE4	6.08e-35	20	186	81	240
QRW16051.1|CE4	6.98e-35	27	180	94	239

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2IW0_A	1.09e-25	1	186	74	247	Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [Colletotrichum lindemuthianum]
7BLY_A	8.55e-25	25	189	82	239	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
2C1I_A	2.95e-19	24	177	278	416	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) D 275 N Mutant. [Streptococcus pneumoniae R6]
2C1G_A	2.95e-19	24	177	278	416	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) [Streptococcus pneumoniae R6]
2Y8U_A	3.61e-19	26	185	76	229	Chain A, CHITIN DEACETYLASE [Aspergillus nidulans],2Y8U_B Chain B, CHITIN DEACETYLASE [Aspergillus nidulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1L3THR9|CDA_PESTX	8.63e-26	1	187	71	238	Chitin deacetylase OS=Pestalotiopsis sp. OX=36460 GN=CDA PE=1 SV=1
sp|Q6DWK3|CDA_COLLN	2.69e-24	1	186	74	247	Chitin deacetylase OS=Colletotrichum lindemuthianum OX=290576 GN=CDA PE=1 SV=1
sp|D4B5F9|PGDA_ARTBC	1.71e-23	20	186	189	349	Probable peptidoglycan-N-acetylglucosamine deacetylase ARB_03699 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03699 PE=1 SV=2
sp|D4AM78|CDA_ARTBC	2.45e-22	20	186	208	368	Chitin deacetylase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=CDA PE=3 SV=1
sp|Q8DP63|PGDA_STRR6	1.69e-18	24	177	310	448	Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000051	0.000006

TMHMM  Annotations     

There is no transmembrane helices in RO3G_01608-t26_1-p1.