CAZyme Information: EEU35211.1

Basic Information

• Species: Fusarium vanettenii
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium vanettenii
• CAZyme ID: EEU35211.1
• CAZy Family: AA7
• CAZyme Description: carbohydrate esterase family 4

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
319	GG698944|CGC1	36839.66	5.8401

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Fvanettenii77134	15708	660122	0	15708

• Gene Location: location=GG698944:126595-127890(-)

Full Sequence      

MGKKKVMVCYGVDIDAVAGWLGSYGGEDSTSDVSRGIWAGTIGTRRLLKLFDKYNIKASW
FIPGHTLESFPEECALVRDAGHEIGLHGYTHENPADMTFEQQRDVLDKTWKLITDFCGGK
PPRGSVAPWWETSAEGTELLLSYGIEYDHSMLHHDCQPYWLRTGDTWTKIDYTKNAEDWM
KPLVKGKETGLVEIPGSWYIDDLPPMMFIKNSANSHGWVNPRRDVEDIWRDHFDYFYREY
DEFIFPMTIHPDVSGRPHVLLMHERIIEHINKHEGVEWVTMAEMADYFKSKNAAPQGGLM
PASKEEAMKRYHEWKKTQS

Enzyme Prediction     

No EC number prediction in EEU35211.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	45	150	1.1e-17	0.7923076923076923

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200563	CE4_HpPgdA_like	2.79e-128	8	289	2	258	Catalytic domain of Helicobacter pylori peptidoglycan deacetylase (HpPgdA) and similar proteins. This family is represented by a peptidoglycan deacetylase (HP0310, HpPgdA) from the gram-negative pathogen Helicobacter pylori. HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. It functions as a homotetramer. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of polysaccharide deacetylase (DCA)-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, HpPgdA does not exhibit a solvent-accessible polysaccharide binding groove, suggesting that the enzyme binds a small molecule at the active site.
213021	CE4_PuuE_HpPgdA_like	3.11e-61	8	287	2	247	Catalytic domain of bacterial PuuE allantoinases, Helicobacter pylori peptidoglycan deacetylase (HpPgdA), and similar proteins. This family is a member of the very large and functionally diverse carbohydrate esterase 4 (CE4) superfamily. It contains bacterial PuuE (purine utilization E) allantoinases, a peptidoglycan deacetylase from Helicobacter pylori (HpPgdA), Escherichia coli ArnD, and many uncharacterized homologs from all three kingdoms of life. PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as a homotetramer. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of polysaccharide deacetylase (DCA)-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. However, in contrast with the typical DCAs, PuuE allantoinase and HpPgdA might not exhibit a solvent-accessible polysaccharide binding groove and only recognize a small substrate molecule. ArnD catalyzes the deformylation of 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol.
200601	CE4_PuuE_like	3.04e-32	36	291	64	281	Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar to bacterial PuuE allantoinases. The family includes a group of uncharacterized prokaryotic polysaccharide deacetylases (DCAs) that show high sequence similarity to the catalytic domain of bacterial PuuE (purine utilization E) allantoinases. PuuE allantoinase specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. It functions as a homotetramer. Its monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCA-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. PuuE allantoinase appears to be metal-independent and acts on a small substrate molecule, which is distinct from the common feature of DCAs which are normally metal ion dependent and recognize multimeric substrates.
200599	CE4_PuuE_SpCDA1	1.36e-20	34	280	58	265	Catalytic domain of bacterial PuuE allantoinases, Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), and similar proteins. Allantoinase (EC 3.5.2.5) can hydrolyze allantoin((2,5-dioxoimidazolidin-4-yl)urea), one of the most important nitrogen carrier for some plants, soil animals, and microorganisms, to allantoate. DAL1 gene from Saccharomyces cerevisiae encodes an allantoinase. However, some organisms possess allantoinase activity but lack DAL1 allantoinase. In those organisms, a defective allantoinase gene, named puuE (purine utilization E), encodes an allantoinase that specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. PuuE allantoinase is related to polysaccharide deacetylase (DCA), one member of the carbohydrate esterase 4 (CE4) superfamily, that removes N-linked or O-linked acetyl groups of cell wall polysaccharides, and lacks sequence similarity with the known DAL1 allantoinase that belongs to the amidohydrolase superfamily. PuuE allantoinase functions as a homotetramer. Its monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCAs. It appears to be metal-independent and acts on a small substrate molecule, which is distinct from the common features of DCAs that are normally metal ion dependent and recognize multimeric substrates. This family also includes a chitin deacetylase 1 (SpCDA1) encoded by the Schizosaccharomyces pombe cda1 gene. Although the general function of chitin deacetylase (CDA) is the synthesis of chitosan from chitin, a polymer of N-acetyl glucosamine, to build up the proper ascospore wall, the actual function of SpCDA1 might involve allantoin hydrolysis. It is likely orthologous to PuuE allantoinase, whereas it is more distantly related to the CDAs found in other fungi, such as Saccharomyces cerevisiae and Mucor rouxii. Those CDAs are similar with rizobial NodB protein and are not included in this family.
200566	CE4_PuuE_HpPgdA_like_2	5.02e-20	24	195	17	172	Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar to bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). This family contains many uncharacterized prokaryotic polysaccharide deacetylases (DCAs) that show high sequence similarity to the catalytic domain of bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as homotetramers. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCA-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, PuuE allantoinase and HpPgdA do not exhibit a solvent-accessible polysaccharide binding groove and might only bind a small molecule at the active site.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UQD84776.1|CE4	1.15e-24	8	285	18	267
ASJ91006.1|CE4	1.89e-17	43	294	62	283
VBB81060.1|CE0	3.29e-14	32	147	30	151
QIS75455.1|CE4	2.48e-13	42	128	168	259
AZR72406.1|CE4	3.33e-13	36	121	63	147

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QBU_A	2.12e-138	4	292	36	322	Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori [Helicobacter pylori G27],3QBU_B Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori [Helicobacter pylori G27],3QBU_C Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori [Helicobacter pylori G27],3QBU_D Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori [Helicobacter pylori G27],4LY4_A Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori [Helicobacter pylori G27],4LY4_B Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori [Helicobacter pylori G27],4LY4_C Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori [Helicobacter pylori G27],4LY4_D Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori [Helicobacter pylori G27]
3RXZ_A	1.55e-23	4	296	23	288	Crystal structure of putative polysaccharide deacetylase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155],3RXZ_B Crystal structure of putative polysaccharide deacetylase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155],3RXZ_C Crystal structure of putative polysaccharide deacetylase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155],3RXZ_D Crystal structure of putative polysaccharide deacetylase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155]
5O6Y_A	2.88e-08	44	126	36	123	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	3.89e-08	44	121	36	113	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]
6HPA_A	4.85e-08	46	125	103	187	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|B5ZA76|PGDAE_HELPG	3.44e-138	4	292	3	289	Peptidoglycan deacetylase OS=Helicobacter pylori (strain G27) OX=563041 GN=pgdA PE=1 SV=1
sp|O25080|PGDAE_HELPY	6.55e-136	4	292	3	289	Peptidoglycan deacetylase OS=Helicobacter pylori (strain ATCC 700392 / 26695) OX=85962 GN=pgdA PE=1 SV=1
sp|I1S2J6|FGM2_GIBZE	1.45e-65	3	295	37	337	Peptidoglycan deacetylase-like protein FGM2 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FGM2 PE=2 SV=1
sp|Q81EK9|PGDA1_BACCR	2.53e-07	44	126	96	183	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000048	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EEU35211.1.