CAZyme Information: KNZ44423.1

Basic Information

• Species: Puccinia sorghi
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia sorghi
• CAZyme ID: KNZ44423.1
• CAZy Family: AA2
• CAZyme Description: NodB homology domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0L6U7D9]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
314		35416.28	8.9831

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsorghiRO10H11247	21769	N/A	691	21078

• Gene Location: location=LAVV01014804:566-2035(-)

Full Sequence      

MVDSWPSTALVLVEAGSARDRAWVNKSKWLDLDSFARFKVQVAMNANFYLCFLMVASCSV
VQSAHHPKASKHVVFSTCSKPGTAAITFDDGPYIYQNKISDYLYERDVKGTFFVNGYNYD
CIYDEDVVKRLRHTFAQGHLIGSHTWSHVNISTLSAHQLHKQLDLTEKALKKILGIKPKF
FRAPYGDFFPSYSGEYNKQSLKVLKQRGYVVVDWSRDSGDSMGASAKKSNAMYTKMAKKF
PSPQIALNHETYKNTAHKVTPHAVEVLQKAGYELMHVSECLGMGAEPEDLYQWVGEPSER
DSSWTCKGTPKPTN

Enzyme Prediction     

EC	3.1.1.72:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	79	212	1.3e-27	0.9153846153846154

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200575	CE4_ClCDA_like	3.30e-79	75	277	1	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	8.03e-42	85	268	4	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.
200569	CE4_SmPgdA_like	8.72e-40	83	273	2	186	Catalytic NodB homology domain of Streptococcus mutans polysaccharide deacetylase PgdA, Bacillus subtilis YheN, and similar proteins. This family is represented by a putative polysaccharide deacetylase PgdA from the oral pathogen Streptococcus mutans (SmPgdA) and Bacillus subtilis YheN (BsYheN), which are members of the carbohydrate esterase 4 (CE4) superfamily. SmPgdA is an extracellular metal-dependent polysaccharide deacetylase with a typical CE4 fold, with metal bound to a His-His-Asp triad. It possesses de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. SmPgdA plays a role in tuning cell surface properties and in interactions with (salivary) agglutinin, an essential component of the innate immune system, most likely through deacetylation of an as-yet-unidentified polysaccharide. SmPgdA shows significant homology to the catalytic domains of peptidoglycan deacetylases from Streptococcus pneumoniae (SpPgdA) and Listeria monocytogenes (LmPgdA), both of which are involved in the bacterial defense mechanism against human mucosal lysozyme. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. The biological function of BsYheN is still unknown. This family also includes many uncharacterized polysaccharide deacetylases mainly found in bacteria.
200578	CE4_CtAXE_like	4.05e-35	85	279	4	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.
396211	Polysacc_deac_1	2.88e-32	78	212	3	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAJ90973.1|CE4	3.30e-112	53	314	12	268
ALL40836.1|CE4	1.56e-81	74	306	54	274
QRV83545.1|CE4	1.89e-67	74	306	37	256
QRV78597.1|CE4	3.03e-67	74	306	31	248
QRW07526.1|CE4	3.44e-66	74	306	31	248

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2IW0_A	3.80e-31	67	292	23	247	Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [Colletotrichum lindemuthianum]
7BLY_A	3.22e-24	74	282	32	228	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
5O6Y_A	9.74e-22	75	226	14	153	Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579]
5O6Y_B	1.34e-20	75	226	14	153	Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579],5O6Y_C Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579],5O6Y_D Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579]
5LFZ_A	1.61e-20	78	291	21	215	T48 deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6DWK3|CDA_COLLN	1.70e-30	67	292	23	247	Chitin deacetylase OS=Colletotrichum lindemuthianum OX=290576 GN=CDA PE=1 SV=1
sp|A0A1L3THR9|CDA_PESTX	3.81e-28	74	282	31	229	Chitin deacetylase OS=Pestalotiopsis sp. OX=36460 GN=CDA PE=1 SV=1
sp|D4AM78|CDA_ARTBC	7.54e-23	74	282	160	360	Chitin deacetylase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=CDA PE=3 SV=1
sp|Q81EK9|PGDA1_BACCR	1.62e-20	75	226	74	213	Peptidoglycan-N-acetylglucosamine deacetylase BC_1960 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_1960 PE=1 SV=1
sp|Q8DP63|PGDA_STRR6	1.09e-19	85	291	271	458	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
0.999813	0.000195

TMHMM  Annotations     

There is no transmembrane helices in KNZ44423.1.