CAZyme Information: PMAA_022650-t26_1-p1

Basic Information

• Species: Talaromyces marneffei
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces marneffei
• CAZyme ID: PMAA_022650-t26_1-p1
• CAZy Family: CE4
• CAZyme Description: polysaccharide deacetylase (NodB), putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
228		25496.33	8.1105

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmarneffeiATCC18224	10194	441960	145	10049

• Gene Location: location=DS995899:1966464-1967262(+)

Full Sequence      

MSLTIDLTRQARSKHATSPIIAPTVIALTIDDAPSVYTTEIFEILKANDAIATFFIIGSH
VSSMEDEGDKILQNLIHGGNELGNHAMYDEPAYKLPDDELVSQINQVDKIIQNAHEAAKG
VPIATADDTAFPRYYRPGHGWYNAKMRSIVSRLRYKLVIGDVYPHDPQIPFARVNAAHIL
RMARPGGIIICHDGRPWTLPMLRSVLPKLKRRGYRIVNVTELLKYADS

Enzyme Prediction     

No EC number prediction in PMAA_022650-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	24	159	5.1e-18	0.9

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200581	CE4_NodB_like_2	3.19e-75	25	222	2	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.
213022	CE4_NodB_like_6s_7s	2.39e-36	25	210	2	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.
200582	CE4_NodB_like_3	2.36e-32	26	217	3	185	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	2.10e-29	25	222	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.
200571	CE4_SpPgdA_BsYjeA_like	1.22e-25	25	219	2	177	Catalytic NodB homology domain of Streptococcus pneumoniae peptidoglycan deacetylase PgdA, Bacillus subtilis BsYjeA protein, and their bacterial homologs. This family is represented by Streptococcus pneumoniae peptidoglycan GlcNAc deacetylase (SpPgdA), a member of the carbohydrate esterase 4 (CE4) superfamily. SpPgdA protects gram-positive bacterial cell wall from host lysozymes by deacetylating peptidoglycan N-acetylglucosamine (GlcNAc) residues. It consists of three separate domains: N-terminal, middle and C-terminal (catalytic) domains. The catalytic NodB homology domain is similar to the deformed (beta/alpha)8 barrel fold adopted by other CE4 esterases, which harbors a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The enzyme is able to accept GlcNAc3 as a substrate, with the N-acetyl of the middle sugar being removed by the enzyme. This family also includes Bacillus subtilis BsYjeA protein encoded by the yjeA gene, which is one of the six polysaccharide deacetylase gene homologs (pdaA, pdaB/ybaN, yheN, yjeA, yxkH and ylxY) in the Bacillus subtilis genome. Although homology comparison shows that the BsYjeA protein contains a polysaccharide deacetylase domain, and was predicted to be a membrane-bound xylanase or a membrane-bound chitooligosaccharide deacetylase, more recent research indicates BsYjeA might be a novel non-specific secretory endonuclease which creates random nicks progressively on the two strands of dsDNA, resulting in highly distinguishable intermediates/products very different in chemical and physical compositions over time. In addition, BsYjeA shares several enzymatic properties with the well-understood DNase I endonuclease. Both enzymes are active on ssDNA and dsDNA, both generate random nicks, and both require Mg2+ or Mn2+ for hydrolytic activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA13072.1|CE4	6.34e-149	25	228	48	251
QKX64722.1|CE4	5.84e-75	25	223	50	239
CAP97257.1|CE4	2.30e-68	25	228	46	238
QDS71316.1|CE4	2.78e-67	25	223	995	1181
QYS98844.1|CE4	1.01e-66	19	223	68	260

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7FBW_A	1.34e-29	26	227	119	304	Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
6HM9_A	1.42e-17	26	223	87	267	Crystal structure of a BA3943 mutant,a CE4 family pseudoenzyme with restored enzymatic activity. [Bacillus anthracis]
5LFZ_A	6.07e-17	26	227	27	208	T48 deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
6H8L_A	6.94e-16	25	222	11	189	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]
6HPA_A	1.69e-15	26	223	88	268	Crystal structure of a BA3943 mutant,a CE4 family pseudoenzyme [Bacillus anthracis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q81AF4|PGDA3_BACCR	1.62e-21	25	225	23	211	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|Q07740|NODB_AZOC5	4.79e-15	26	216	17	206	Chitooligosaccharide deacetylase OS=Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB 13405 / ORS 571) OX=438753 GN=nodB PE=3 SV=2
sp|O34798|PDAC_BACSU	2.49e-14	25	222	279	457	Peptidoglycan-N-acetylmuramic acid deacetylase PdaC OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaC PE=1 SV=1
sp|P04339|NODB_RHILV	5.23e-14	26	216	23	212	Chitooligosaccharide deacetylase OS=Rhizobium leguminosarum bv. viciae OX=387 GN=nodB PE=3 SV=1
sp|Q5AQQ0|CDA_EMENI	9.92e-14	5	223	21	228	Chitin deacetylase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=cda PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000080	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PMAA_022650-t26_1-p1.