CAZyme Information: KIX03419.1

Basic Information

• Species: Rhinocladiella mackenziei
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Rhinocladiella; Rhinocladiella mackenziei
• CAZyme ID: KIX03419.1
• CAZy Family: GH13
• CAZyme Description: NodB homology domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0D2IC79]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
241	KN847479|CGC1	27405.98	9.3424

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RmackenzieiCBS650.93	11418	1442369	36	11382

• Gene Location: location=KN847479:1369841-1370566(+)

Full Sequence      

MSILFLFLIVFSFIIFPLLYIIYKPPACLIQLLTRRWPDVLFQLSIKQRIVALTIDDGPS
PYTSAIQHILDTSGAKATFFVIGSHIPGHENILTNLILNNHELANHAVRDEPSRSLPTAE
LISQIKCVESQVGAIYASLHRQAAQPRYFRPGSGFFSTSMRQVLRDLDYRLVLGNIYPHD
AQISFWRLNAWHILSMVRPGGIIVCHDRKWTPSMLRTVLPELKRRGYEVVTVTELLNAAE
S

Enzyme Prediction     

No EC number prediction in KIX03419.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	47	174	3.5e-18	0.9230769230769231

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200581	CE4_NodB_like_2	1.60e-72	49	235	1	190	Catalytic NodB homology domain of uncharacterized chitin deacetylases and hypothetical proteins. This family includes some uncharacterized chitin deacetylases and hypothetical proteins, mainly from eukaryotes. Although their biological function is unknown, members in this family show high sequence homology to the catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41), which catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. Like ClCDA, this family is a member the carbohydrate esterase 4 (CE4) superfamily.
200582	CE4_NodB_like_3	3.06e-36	49	232	1	187	Catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases. This family includes many uncharacterized bacterial polysaccharide deacetylases. Although their biological function still remains unknown, members in this family show high sequence homology to the catalytic NodB homology domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), which is an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Like SpPgdA, this family is a member of the carbohydrate esterase 4 (CE4) superfamily.
200578	CE4_CtAXE_like	1.12e-35	50	235	2	180	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.
213022	CE4_NodB_like_6s_7s	4.37e-35	49	223	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.
200580	CE4_BH1302_like	6.55e-26	48	236	4	193	Putative catalytic NodB homology domain of uncharacterized BH1302 protein from Bacillus halodurans and its bacterial homologs. This family is represented by a putative polysaccharide deacetylase BH1302 from Bacillus halodurans. Although its biological function is unknown, BH1302 shows high sequence homology to the catalytic NodB homology domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), which is an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Both BH1302 and SpPgdA belong to the carbohydrate esterase 4 (CE4) superfamily. This family also includes many uncharacterized bacterial polysaccharide deacetylases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UDD61559.1|CE4	5.09e-85	20	238	16	237
QMW41954.1|CE4	5.09e-85	20	238	16	237
QMW29882.1|CE4	5.09e-85	20	238	16	237
BAE60108.1|CE4	8.06e-85	20	238	30	251
QRD86297.1|CE4	8.06e-85	20	238	30	251

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7FBW_A	5.92e-24	51	236	119	300	Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
7AX7_A	1.75e-17	48	235	3	185	Crystal structure of the Xyl-CE4 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides [uncultured bacterium]
7BLY_A	1.03e-16	51	241	42	232	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
2Y8U_A	2.37e-16	51	240	35	225	Chain A, CHITIN DEACETYLASE [Aspergillus nidulans],2Y8U_B Chain B, CHITIN DEACETYLASE [Aspergillus nidulans]
2C1G_A	3.80e-16	48	237	235	417	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q81AF4|PGDA3_BACCR	1.58e-21	40	236	13	209	Peptidoglycan-N-acetylglucosamine deacetylase BC_3618 OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=BC_3618 PE=1 SV=1
sp|D4B5F9|PGDA_ARTBC	4.30e-16	51	236	151	340	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|P83513|XY11A_PSEXY	7.31e-16	48	235	401	583	Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A PE=1 SV=2
sp|Q5AQQ0|CDA_EMENI	1.37e-15	51	240	42	232	Chitin deacetylase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=cda PE=1 SV=1
sp|P04675|NODB_BRASP	1.41e-15	49	235	21	218	Chitooligosaccharide deacetylase OS=Bradyrhizobium sp. (strain ANU 289) OX=186901 GN=nodB PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000031	0.000004

TMHMM  Annotations     

Start	End
2	23