CAZyme Information: MGYG000001384_03558

Basic Information

• Species: Ralstonia pickettii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Ralstonia; Ralstonia pickettii
• CAZyme ID: MGYG000001384_03558
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
320	MGYG000001384_3|CGC3	36557.05	6.2217

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001384	5243975	Isolate	not provided	not provided

• Gene Location: Start: 452761; End: 453723 Strand: +

Full Sequence      

MTNNNYPRDLIGYGKNPPNANWPGGARVALQFVLNYEEGGENCVLHGDAGSEQFLSEIIG
AAAYPARHMSMEGIYEYGSRAGVWRILREFEKRGLPLTIFGVSMALQRHPDVTQAFVDLG
HEIACHGWRWIHYQNIDEATEREHMRIGVEIIRELTGNAPLGWYTGRDSPNTRRLVVEHG
GFAYDADYYGDDLPFWTEVETSSGEHKPHLVVPYTLDTNDMRFASPQGFNTADHFYQYLK
DAFDVLYEEGDPNGLAQPKMLSIGMHCRLLGRPARFRALQRFLDYVQSHDKVWICRRIDI
AQHWIQNHPYAKQPVLSTTA

Enzyme Prediction     

EC	3.5.1.41

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR03212	uraD_N-term-dom	0.0	6	310	1	297	putative urate catabolism protein. This model represents a protein that is predominantly found just upstream of the UraD protein (OHCU decarboxylase) and in a number of instances as a N-terminal fusion with it. UraD itself catalyzes the last step in the catabolism of urate to allantoate. The function of this protein is presently unknown. It shows homology with the pfam01522 polysaccharide deacetylase domain family.
cd10977	CE4_PuuE_SpCDA1	0.0	22	303	1	273	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.
cd10980	CE4_SpCDA1	1.80e-114	22	310	1	297	Putative catalytic domain of Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), and similar proteins. This family is represented by Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), encoded by the cda1 gene. 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 be involved in allantoin hydrolysis. It is likely an ortholog to bacterial 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.
cd10916	CE4_PuuE_HpPgdA_like	3.77e-75	29	303	1	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.
cd10978	CE4_Sll1306_like	4.12e-60	22	309	2	271	Putative catalytic domain of Synechocystis sp. Sll1306 protein and other bacterial homologs. The family contains Synechocystis sp. Sll1306 protein and uncharacterized bacterial polysaccharide deacetylases. Although their biological function remains unknown, they show very high sequence homology 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 polysaccharide deacetylase-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 polysaccharide deacetylases that are normally metal ion dependent and recognize multimeric substrates.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQK35724.1	9.25e-250	1	320	1	320
ANJ71835.1	1.72e-245	1	320	1	320
ANH73633.1	3.47e-245	1	320	1	320
ATG19449.1	7.85e-242	1	320	1	320
ANA32416.1	7.85e-242	1	320	1	320

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3S6O_A	5.08e-187	5	310	10	311	Crystalstructure of a Polysaccharide deacetylase family protein from Burkholderia pseudomallei [Burkholderia pseudomallei],3S6O_B Crystal structure of a Polysaccharide deacetylase family protein from Burkholderia pseudomallei [Burkholderia pseudomallei],3S6O_C Crystal structure of a Polysaccharide deacetylase family protein from Burkholderia pseudomallei [Burkholderia pseudomallei],3S6O_D Crystal structure of a Polysaccharide deacetylase family protein from Burkholderia pseudomallei [Burkholderia pseudomallei]
3CL6_A	1.02e-148	6	310	5	303	Crystalstructure of Puue Allantoinase [Pseudomonas fluorescens],3CL6_B Crystal structure of Puue Allantoinase [Pseudomonas fluorescens],3CL7_A Crystal structure of Puue Allantoinase in complex with Hydantoin [Pseudomonas fluorescens],3CL7_B Crystal structure of Puue Allantoinase in complex with Hydantoin [Pseudomonas fluorescens],3CL8_A Crystal structure of Puue Allantoinase complexed with ACA [Pseudomonas fluorescens],3CL8_B Crystal structure of Puue Allantoinase complexed with ACA [Pseudomonas fluorescens]
1Z7A_A	1.12e-145	6	310	5	303	Crystalstructure of probable Polysaccharide deacetylase from Pseudomonas aeruginosa PAO1 [Pseudomonas aeruginosa PAO1],1Z7A_B Crystal structure of probable Polysaccharide deacetylase from Pseudomonas aeruginosa PAO1 [Pseudomonas aeruginosa PAO1],1Z7A_C Crystal structure of probable Polysaccharide deacetylase from Pseudomonas aeruginosa PAO1 [Pseudomonas aeruginosa PAO1],1Z7A_D Crystal structure of probable Polysaccharide deacetylase from Pseudomonas aeruginosa PAO1 [Pseudomonas aeruginosa PAO1],1Z7A_E Crystal structure of probable Polysaccharide deacetylase from Pseudomonas aeruginosa PAO1 [Pseudomonas aeruginosa PAO1],1Z7A_F Crystal structure of probable Polysaccharide deacetylase from Pseudomonas aeruginosa PAO1 [Pseudomonas aeruginosa PAO1],1Z7A_G Crystal structure of probable Polysaccharide deacetylase from Pseudomonas aeruginosa PAO1 [Pseudomonas aeruginosa PAO1],1Z7A_H Crystal structure of probable Polysaccharide deacetylase from Pseudomonas aeruginosa PAO1 [Pseudomonas aeruginosa PAO1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O13842	1.90e-87	8	310	5	318	Putative polysaccharide deacetylase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=cda1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000060	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001384_03558.