CAZyme Information: MGYG000002827_04334

Basic Information

• Species: Phyllobacterium sp900539805
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales_A; Rhizobiaceae_A; Phyllobacterium; Phyllobacterium sp900539805
• CAZyme ID: MGYG000002827_04334
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
305	MGYG000002827_52|CGC1	34697.08	5.7683

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002827	5102924	MAG	Singapore	Asia

• Gene Location: Start: 19413; End: 20330 Strand: +

Full Sequence      

MSDYPRDLIGFGRNTPDPKWPGHARIAVQFVINYEEGGESCILDNDPASENLLSEIVGAA
AWPGQRNLNMESIYEYGSRAGFWRLWRIFTRRNLPVTVYGVTLAMARNPEAVAAMQEADW
EIASHGLRWLEYKDFPEDIERQHILEAVRLHTEITGARPLGIYQGKPSDNTLKIVMEEGG
FVYSADSYADELPYWVKGPKGPHLIVPYTLDANDMRFATPQGFNTGDQFFTYLKDTFDVL
YREGQEGAAKMMSVGLHCRLVGRPGRAAALERFLDYVQGHEAAWVTRRIDIARHWHEHHR
PDSAV

Enzyme Prediction     

No EC number prediction in MGYG000002827_04334.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR03212	uraD_N-term-dom	0.0	4	301	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	2.99e-164	20	294	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	4.67e-103	20	299	1	295	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	2.25e-59	27	294	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.
cd10979	CE4_PuuE_like	2.79e-49	16	298	10	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND52263.1	7.98e-223	1	305	1	305
ATU93838.1	2.75e-217	1	305	1	305
ASV85413.1	7.43e-202	4	304	3	303
QWK77987.1	3.01e-201	4	301	3	300
ANG95272.1	3.01e-201	4	301	3	300

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3CL6_A	1.84e-133	3	305	4	307	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]
3S6O_A	2.04e-133	3	299	10	309	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]
1Z7A_A	4.69e-129	2	299	3	301	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]
3RXZ_A	1.38e-12	20	294	19	279	Crystalstructure 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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O13842	4.49e-79	6	299	5	316	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
1.000063	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002827_04334.